|
Name |
Accession |
Description |
Interval |
E-value |
| ASKHA_NBD_FGGY_GK1-3-like |
cd07792 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 1-3 (GK1-3) and similar proteins; ... |
11-544 |
0e+00 |
|
nucleotide-binding domain (NBD) of metazoan glycerol kinase 1-3 (GK1-3) and similar proteins; This subfamily contains metazoan glycerol kinases (GKs), coded by X chromosome-linked GK genes, and glycerol kinase (GK)-like proteins, coded by autosomal testis-specific GK-like genes (GK-like genes, GK2 and GK3). Sequence comparison shows that metazoan GKs and GK-like proteins in this family are closely related to the bacterial GKs (EC 2.7.1.30), which catalyze the Mg-ATP dependent phosphorylation of glycerol to yield glycerol 3-phosphate (G3P). The metazoan GKs do have GK enzymatic activity. However, the GK-like metazoan proteins do not exhibit GK activity and their biological functions are not yet clear. Some of them lack important functional residues involved in the binding of ADP and Mg2+, which may result in the loss of GK catalytic function. Others that have conserved catalytic residues have lost their GK activity as well; the reason remains unclear. It has been suggested the conserved catalytic residues might facilitate them performing a distinct function. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466802 [Multi-domain] Cd Length: 499 Bit Score: 982.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 11 PLVGAVDQGTSSTRFLVFNSkTAELLSHHQVEIKQEFPREGWVEQDPKEILQSVYECIEKTCEKLGQLNIDISNIKAIGV 90
Cdd:cd07792 1 PLVGAIDQGTTSTRFIVFDS-TGELVASHQVEHKQIYPKPGWVEHDPMEILESVYECIEEAVEKLKALGISPSDIKAIGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 91 SNQRETTVVWDKLTGEPLYNAVaapvspgssvpvavvpsgspvpaagassVWLDLRTQSTVEKLSKRIPGNNNFVKSKTG 170
Cdd:cd07792 80 TNQRETTVVWDKSTGKPLYNAI----------------------------VWLDTRTSDTVEELSAKTPGGKDHFRKKTG 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 171 LPLSTYFSAVKLRWLLDNVKKVQEAVEENRALFGTIDSWLIWSLTGGINGGVHCTDVTNASRTMLFNIHSLEWDKELCEF 250
Cdd:cd07792 132 LPISTYFSAVKLRWLLDNVPEVKKAVDDGRLLFGTVDSWLIWNLTGGKNGGVHVTDVTNASRTMLMNLRTLQWDPELCEF 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 251 FGIPMEILPNVRSSSEIYGLMKIshslkaGALEGVPISGCLGDQSAALVGQMCFQDGQAKNTYGTGCFLLCNTGHKCVFS 330
Cdd:cd07792 212 FGIPMSILPEIRSSSEVYGKIAS------GPLAGVPISGCLGDQQAALVGQGCFKPGEAKNTYGTGCFLLYNTGEEPVFS 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 331 EHGLLTTVAYKLGRDKPVYYALEGSVAIAGAVIRWLRDNLGIIKSSEEIEKLAKEVGTSYGCYFVPAFSGLYAPYWEPSA 410
Cdd:cd07792 286 KHGLLTTVAYKLGPDAPPVYALEGSIAIAGAAVQWLRDNLGIISSASEVETLAASVPDTGGVYFVPAFSGLFAPYWRPDA 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 411 RGIICGLTQFTNKCHIAFAALEAVCFQTREILDAMNRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPETTA 490
Cdd:cd07792 366 RGTIVGLTQFTTKAHIARAALEAVCFQTREILDAMNKDSGIPLTSLRVDGGMTKNNLLMQIQADILGIPVERPSMVETTA 445
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1958808298 491 LGAAMAAGAAEGVGVWSLEPEDLSAVTMERFEPQINAEESEIRYSTWKKAVMKS 544
Cdd:cd07792 446 LGAAIAAGLAVGVWKSLDELKSLNEGGRTVFEPQISEEERERRYKRWKKAVERS 499
|
|
| glycerol_kin |
TIGR01311 |
glycerol kinase; This model describes glycerol kinase, a member of the FGGY family of ... |
11-547 |
0e+00 |
|
glycerol kinase; This model describes glycerol kinase, a member of the FGGY family of carbohydrate kinases. [Energy metabolism, Other]
Pssm-ID: 273549 [Multi-domain] Cd Length: 493 Bit Score: 813.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 11 PLVGAVDQGTSSTRFLVFNsKTAELLSHHQVEIKQEFPREGWVEQDPKEILQSVYECIEKTCEKLGqlnIDISNIKAIGV 90
Cdd:TIGR01311 1 PYILAIDQGTTSSRAIVFD-KDGNIVAIHQKEFTQIFPKPGWVEHDPMEIWESVLSCIAEALAKAG---IKPDDIAAIGI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 91 SNQRETTVVWDKLTGEPLYNAVaapvspgssvpvavvpsgspvpaagassVWLDLRTQSTVEKLSKRIPGNnnFVKSKTG 170
Cdd:TIGR01311 77 TNQRETTVVWDKATGKPLYNAI----------------------------VWQDRRTASICEELKAEGYGE--FIREKTG 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 171 LPLSTYFSAVKLRWLLDNVKKVQEAVEENRALFGTIDSWLIWSLTGGingGVHCTDVTNASRTMLFNIHSLEWDKELCEF 250
Cdd:TIGR01311 127 LPLDPYFSATKLRWLLDNVPGVREAAERGELLFGTIDTWLIWNLTGG---KVHVTDVTNASRTMLFNIHTLDWDDELLEL 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 251 FGIPMEILPNVRSSSEIYGLMKISHSLkagalEGVPISGCLGDQSAALVGQMCFQDGQAKNTYGTGCFLLCNTGHKCVFS 330
Cdd:TIGR01311 204 FGIPREILPEVRSSSEVYGYTDPGLLG-----AEIPITGVLGDQQAALFGQACFKPGQAKNTYGTGCFLLMNTGEKPVIS 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 331 EHGLLTTVAYKLGRDKPVYyALEGSVAIAGAVIRWLRDNLGIIKSSEEIEKLAKEVGTSYGCYFVPAFSGLYAPYWEPSA 410
Cdd:TIGR01311 279 KHGLLTTVAYQLGGKKPVY-ALEGSVFVAGAAVQWLRDNLKLIKHAAESEALARSVEDNGGVYFVPAFTGLGAPYWDPDA 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 411 RGIICGLTQFTNKCHIAFAALEAVCFQTREILDAMNRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPETTA 490
Cdd:TIGR01311 358 RGAIFGLTRGTTKAHIARAALEAIAFQTRDVLEAMEKDAGVEITKLRVDGGMTNNNLLMQFQADILGVPVVRPKVTETTA 437
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958808298 491 LGAAMAAGAAEGVGVWSLEPEDLSAVTmERFEPQINAEESEIRYSTWKKAVMKSIGW 547
Cdd:TIGR01311 438 LGAAYAAGLAVGYWKSLEEIEALWRVE-KTFEPEMDEEEREARYAGWKEAVKRSLGW 493
|
|
| ASKHA_NBD_FGGY_GK |
cd07769 |
nucleotide-binding domain (NBD) of glycerol kinase (GK) and similar proteins; GK (EC 2.7.1.30), ... |
13-541 |
0e+00 |
|
nucleotide-binding domain (NBD) of glycerol kinase (GK) and similar proteins; GK (EC 2.7.1.30), also called ATP:glycerol 3-phosphotransferase, or glycerokinase, is a key enzyme in the regulation of glycerol uptake and metabolism. It catalyzes the Mg-ATP-dependent phosphorylation of glycerol to yield sn-glycerol 3-phosphate. It also catalyzes the phosphorylation of dihydroxyacetone, L-glyceraldehyde and D-glyceraldehyde. The subfamily includes GKs and GK-like proteins from all three kingdoms of living organisms. Metazoan GKs, coded by X chromosome-linked GK genes, and GK-like proteins, coded by autosomal testis-specific GK-like genes GK2, GK3 and Gykl1 (in mouse) are closely related to the bacterial GKs. The metazoan GKs do have GK enzymatic activity. However, the GK-like metazoan proteins do not exhibit GK activity and their biological functions are not yet clear. Some of them lack important functional residues involved in the binding of ADP and Mg2+, which may result in the loss of GK catalytic function. Others that have conserved catalytic residues have lost their GK activity as well; the reason remains unclear. It has been suggested the conserved catalytic residues might facilitate them performing a distinct function. Under different conditions, GKs from different species may exist in different oligomeric states. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466789 [Multi-domain] Cd Length: 486 Bit Score: 747.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 13 VGAVDQGTSSTRFLVFNSKtAELLSHHQVEIKQEFPREGWVEQDPKEILQSVYECIEKTCEKLGqlnIDISNIKAIGVSN 92
Cdd:cd07769 2 ILAIDQGTTSTRAILFDED-GNIVASAQKEHEQIYPQPGWVEHDPEEIWENTLEVIREALAKAG---ISASDIAAIGITN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 93 QRETTVVWDKLTGEPLYNAVaapvspgssvpvavvpsgspvpaagassVWLDLRTQSTVEKLSKRipGNNNFVKSKTGLP 172
Cdd:cd07769 78 QRETTVVWDKKTGKPLYNAI----------------------------VWQDRRTADICEELKAK--GLEERIREKTGLP 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 173 LSTYFSAVKLRWLLDNVKKVQEAVEENRALFGTIDSWLIWSLTGGingGVHCTDVTNASRTMLFNIHSLEWDKELCEFFG 252
Cdd:cd07769 128 LDPYFSATKIKWILDNVPGARERAERGELLFGTIDTWLIWKLTGG---KVHVTDVTNASRTMLFNIHTLEWDDELLELFG 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 253 IPMEILPNVRSSSEIYGlmkisHSLKAGALEGVPISGCLGDQSAALVGQMCFQDGQAKNTYGTGCFLLCNTGHKCVFSEH 332
Cdd:cd07769 205 IPRSMLPEVRPSSEVFG-----YTDPEGLGAGIPIAGILGDQQAALFGQGCFEPGMAKNTYGTGCFLLMNTGEKPVPSKN 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 333 GLLTTVAYKLgrDKPVYYALEGSVAIAGAVIRWLRDNLGIIKSSEEIEKLAKEVGTSYGCYFVPAFSGLYAPYWEPSARG 412
Cdd:cd07769 280 GLLTTIAWQI--GGKVTYALEGSIFIAGAAIQWLRDNLGLIEDAAETEELARSVEDNGGVYFVPAFSGLGAPYWDPDARG 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 413 IICGLTQFTNKCHIAFAALEAVCFQTREILDAMNRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPETTalg 492
Cdd:cd07769 358 AIVGLTRGTTKAHIVRAALESIAYQTRDVLEAMEKDSGIKLKELRVDGGATANNFLMQFQADILGVPVVRPKVAETTalg 437
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1958808298 493 aamaagaaegvgVWSLEPEDLSAVTMER-FEPQINAEESEIRYSTWKKAV 541
Cdd:cd07769 438 aayl--aglavgFWKDLDELASLWQVDKrFEPSMDEEERERLYRGWKKAV 485
|
|
| GlpK |
COG0554 |
Glycerol kinase [Energy production and conversion]; |
13-548 |
0e+00 |
|
Glycerol kinase [Energy production and conversion];
Pssm-ID: 440320 [Multi-domain] Cd Length: 496 Bit Score: 741.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 13 VGAVDQGTSSTRFLVFNSKtAELLSHHQVEIKQEFPREGWVEQDPKEILQSVYECIEKTCEKLGqlnIDISNIKAIGVSN 92
Cdd:COG0554 5 ILAIDQGTTSTRAILFDRD-GNIVAVAQREFTQIYPQPGWVEHDPEEIWESVLAVIREALAKAG---ISAEDIAAIGITN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 93 QRETTVVWDKLTGEPLYNAVaapvspgssvpvavvpsgspvpaagassVWLDLRTQSTVEKLSKRipGNNNFVKSKTGLP 172
Cdd:COG0554 81 QRETTVVWDRKTGKPLYNAI----------------------------VWQDRRTADICEELKAD--GLEDLIREKTGLV 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 173 LSTYFSAVKLRWLLDNVKKVQEAVEENRALFGTIDSWLIWSLTGGingGVHCTDVTNASRTMLFNIHSLEWDKELCEFFG 252
Cdd:COG0554 131 LDPYFSATKIKWILDNVPGARERAEAGELLFGTIDSWLIWKLTGG---KVHVTDVTNASRTMLFNIHTLDWDDELLELFG 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 253 IPMEILPNVRSSSEIYGlmkisHSLKAGALEGVPISGCLGDQSAALVGQMCFQDGQAKNTYGTGCFLLCNTGHKCVFSEH 332
Cdd:COG0554 208 IPRSMLPEVRPSSEVFG-----ETDPDLFGAEIPIAGIAGDQQAALFGQACFEPGMAKNTYGTGCFLLMNTGDEPVRSKN 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 333 GLLTTVAYKLGrDKPVYyALEGSVAIAGAVIRWLRDNLGIIKSSEEIEKLAKEVGTSYGCYFVPAFSGLYAPYWEPSARG 412
Cdd:COG0554 283 GLLTTIAWGLG-GKVTY-ALEGSIFVAGAAVQWLRDGLGLIDSAAESEALARSVEDNGGVYFVPAFTGLGAPYWDPDARG 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 413 IICGLTQFTNKCHIAFAALEAVCFQTREILDAMNRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPETTalg 492
Cdd:COG0554 361 AIFGLTRGTTRAHIARAALESIAYQTRDVLDAMEADSGIPLKELRVDGGASANDLLMQFQADILGVPVERPKVTETTalg 440
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958808298 493 aamaagaaegvgVWSlEPEDLSAV--TMERFEPQINAEESEIRYSTWKKAVMKSIGWV 548
Cdd:COG0554 441 aayl--aglavgFWK-SLEELAALwkVDRRFEPQMDEEERERLYAGWKKAVERTLGWA 495
|
|
| PTZ00294 |
PTZ00294 |
glycerol kinase-like protein; Provisional |
11-548 |
0e+00 |
|
glycerol kinase-like protein; Provisional
Pssm-ID: 240348 [Multi-domain] Cd Length: 504 Bit Score: 712.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 11 PLVGAVDQGTSSTRFLVFNSKtAELLSHHQVEIKQEFPREGWVEQDPKEILQSVYECIEKTCEKLGQLNIDISnIKAIGV 90
Cdd:PTZ00294 2 KYIGSIDQGTTSTRFIIFDEK-GNVVSSHQIPHEQITPHPGWLEHDPEEILRNVYKCMNEAIKKLREKGPSFK-IKAIGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 91 SNQRETTVVWDKLTGEPLYNAVaapvspgssvpvavvpsgspvpaagassVWLDLRTQSTVEKLSKRIPGNNNFVKsKTG 170
Cdd:PTZ00294 80 TNQRETVVAWDKVTGKPLYNAI----------------------------VWLDTRTYDIVNELTKKYGGSNFFQK-ITG 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 171 LPLSTYFSAVKLRWLLDNVKKVQEAVEENRALFGTIDSWLIWSLTGGingGVHCTDVTNASRTMLFNIHSLEWDKELCEF 250
Cdd:PTZ00294 131 LPISTYFSAFKIRWMLENVPAVKDAVKEGTLLFGTIDTWLIWNLTGG---KSHVTDVTNASRTFLMNIKTLKWDEELLNK 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 251 FGIPMEILPNVRSSSEIYGLMKishSLKAGALEGVPISGCLGDQSAALVGQMCFQDGQAKNTYGTGCFLLCNTGHKCVFS 330
Cdd:PTZ00294 208 FGIPKETLPEIKSSSENFGTIS---GEAVPLLEGVPITGCIGDQQAALIGHGCFEKGDAKNTYGTGCFLLMNTGTEIVFS 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 331 EHGLLTTVAYKLGRDKPVYYALEGSVAIAGAVIRWLRDNLGIIKSSEEIEKLAKEVGTSYGCYFVPAFSGLYAPYWEPSA 410
Cdd:PTZ00294 285 KHGLLTTVCYQLGPNGPTVYALEGSIAVAGAGVEWLRDNMGLISHPSEIEKLARSVKDTGGVVFVPAFSGLFAPYWRPDA 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 411 RGIICGLTQFTNKCHIAFAALEAVCFQTREILDAMNRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPETTa 490
Cdd:PTZ00294 365 RGTIVGMTLKTTRAHIVRAALEAIALQTNDVIESMEKDAGIELNSLRVDGGLTKNKLLMQFQADILGKDIVVPEMAETT- 443
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 491 lGAAMAAGAAEGVGVW-SLEP-EDLSAVTMERFEPQINAEESEIRYSTWKKAVMKSIGWV 548
Cdd:PTZ00294 444 -ALGAALLAGLAVGVWkSLEEvKKLIRRSNSTFSPQMSAEERKAIYKEWNKAVERSLKWA 502
|
|
| PLN02295 |
PLN02295 |
glycerol kinase |
12-548 |
0e+00 |
|
glycerol kinase
Pssm-ID: 215166 [Multi-domain] Cd Length: 512 Bit Score: 698.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 12 LVGAVDQGTSSTRFLVFNsKTAELLSHHQVEIKQEFPREGWVEQDPKEILQSVYECIEKTCEKLGQ--LNIDiSNIKAIG 89
Cdd:PLN02295 1 FVGAIDQGTTSTRFIIYD-RDARPVASHQVEFTQIYPQAGWVEHDPMEILESVLTCIAKALEKAAAkgHNVD-SGLKAIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 90 VSNQRETTVVWDKLTGEPLYNAVaapvspgssvpvavvpsgspvpaagassVWLDLRTQSTVEKLSKRIPGNNNFVKSKT 169
Cdd:PLN02295 79 ITNQRETTVAWSKSTGRPLYNAI----------------------------VWMDSRTSSICRRLEKELSGGRKHFVETC 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 170 GLPLSTYFSAVKLRWLLDNVKKVQEAVEENRALFGTIDSWLIWSLTGGINGGVHCTDVTNASRTMLFNIHSLEWDKELCE 249
Cdd:PLN02295 131 GLPISTYFSATKLLWLLENVDAVKEAVKSGDALFGTIDSWLIWNLTGGASGGVHVTDVTNASRTMLMNLKTLDWDKPTLE 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 250 FFGIPMEILPNVRSSSEIYGlmKISHSlkaGALEGVPISGCLGDQSAALVGQMCfQDGQAKNTYGTGCFLLCNTGHKCVF 329
Cdd:PLN02295 211 ALGIPAEILPKIVSNSEVIG--TIAKG---WPLAGVPIAGCLGDQHAAMLGQRC-RPGEAKSTYGTGCFILLNTGEEVVP 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 330 SEHGLLTTVAYKLGRDKPVYYALEGSVAIAGAVIRWLRDNLGIIKSSEEIEKLAKEVGTSYGCYFVPAFSGLYAPYWEPS 409
Cdd:PLN02295 285 SKHGLLTTVAYKLGPDAPTNYALEGSVAIAGAAVQWLRDNLGIIKSASEIEALAATVDDTGGVYFVPAFSGLFAPRWRDD 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 410 ARGIICGLTQFTNKCHIAFAALEAVCFQTREILDAMNRDCGIPLSH-----LQVDGGMTSNKILMQLQADILYIPVVKPS 484
Cdd:PLN02295 365 ARGVCVGITRFTNKAHIARAVLESMCFQVKDVLDAMRKDAGEEKSHkglflLRVDGGATANNLLMQIQADLLGSPVVRPA 444
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958808298 485 MPETTalGAAMAAGAAEGVGVWSlePEDLSAVTMER----FEPQINAEESEIRYSTWKKAVMKSIGWV 548
Cdd:PLN02295 445 DIETT--ALGAAYAAGLAVGLWT--EEEIFASEKWKntttFRPKLDEEERAKRYASWCKAVERSFDLA 508
|
|
| glpK |
PRK00047 |
glycerol kinase GlpK; |
13-548 |
0e+00 |
|
glycerol kinase GlpK;
Pssm-ID: 234594 [Multi-domain] Cd Length: 498 Bit Score: 688.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 13 VGAVDQGTSSTRFLVFNsKTAELLSHHQVEIKQEFPREGWVEQDPKEILQSVYECIEktcEKLGQLNIDISNIKAIGVSN 92
Cdd:PRK00047 7 ILALDQGTTSSRAIIFD-HDGNIVSVAQKEFTQIFPQPGWVEHDPNEIWASQLSVIA---EALAKAGISPDQIAAIGITN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 93 QRETTVVWDKLTGEPLYNAVaapvspgssvpvavvpsgspvpaagassVWLDLRTQSTVEKLSKRipGNNNFVKSKTGLP 172
Cdd:PRK00047 83 QRETTVVWDKETGRPIYNAI----------------------------VWQDRRTADICEELKRD--GYEDYIREKTGLV 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 173 LSTYFSAVKLRWLLDNVKKVQEAVEENRALFGTIDSWLIWSLTGGingGVHCTDVTNASRTMLFNIHSLEWDKELCEFFG 252
Cdd:PRK00047 133 IDPYFSGTKIKWILDNVEGARERAEKGELLFGTIDTWLVWKLTGG---KVHVTDYTNASRTMLFNIHTLDWDDELLELLD 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 253 IPMEILPNVRSSSEIYGLMKISHSLKAGalegVPISGCLGDQSAALVGQMCFQDGQAKNTYGTGCFLLCNTGHKCVFSEH 332
Cdd:PRK00047 210 IPRSMLPEVRPSSEVYGKTNPYGFFGGE----VPIAGIAGDQQAALFGQLCFEPGMAKNTYGTGCFMLMNTGEKAVKSEN 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 333 GLLTTVAYKLGrDKPVYyALEGSVAIAGAVIRWLRDNLGIIKSSEEIEKLAKEVGTSYGCYFVPAFSGLYAPYWEPSARG 412
Cdd:PRK00047 286 GLLTTIAWGID-GKVVY-ALEGSIFVAGSAIQWLRDGLKIISDASDSEALARKVEDNDGVYVVPAFTGLGAPYWDSDARG 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 413 IICGLTQFTNKCHIAFAALEAVCFQTREILDAMNRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPETTalg 492
Cdd:PRK00047 364 AIFGLTRGTTKEHIIRATLESIAYQTRDVLDAMQADSGIRLKELRVDGGAVANNFLMQFQADILGVPVERPVVAETT--- 440
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958808298 493 aamaagaaegvgvwSL--------------EPEDLSAVTME--RFEPQINAEESEIRYSTWKKAVMKSIGWV 548
Cdd:PRK00047 441 --------------ALgaaylaglavgfwkDLDELKEQWKIdrRFEPQMDEEEREKLYAGWKKAVKRTLAWA 498
|
|
| FGGY_EcGK_like |
cd07786 |
Escherichia coli glycerol kinase-like proteins; belongs to the FGGY family of carbohydrate ... |
15-541 |
0e+00 |
|
Escherichia coli glycerol kinase-like proteins; belongs to the FGGY family of carbohydrate kinases; This subgroup is composed of mostly bacterial and archaeal glycerol kinases (GK), including the well characterized proteins from Escherichia coli (EcGK), Thermococcus kodakaraensis (TkGK), and Enterococcus casseliflavus (EnGK). GKs contain two large domains separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain. The high affinity ATP binding site of EcGK is created only by a substrate-induced conformational change, which is initiated by protein-protein interactions through complex formation with enzyme IIAGlc (also known as IIIGlc), the glucose-specific phosphocarrier protein of the phosphotransferase system (PTS). EcGK exists in a dimer-tetramer equilibrium. IIAGlc binds to both EcGK dimer and tetramer, and inhibits the uptake and subsequent metabolism of glycerol and maltose. Another well-known allosteric regulator of EcGK is fructose 1,6-bisphosphate (FBP), which binds to the EcGK tetramer and plays an essential role in the stabilization of the inactive tetrameric form. EcGK requires Mg2+ for its enzymatic activity. Members in this subgroup belong to the FGGY family of carbohydrate kinases
Pssm-ID: 198361 [Multi-domain] Cd Length: 486 Bit Score: 682.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 15 AVDQGTSSTRFLVFNsKTAELLSHHQVEIKQEFPREGWVEQDPKEILQSVYECIEktcEKLGQLNIDISNIKAIGVSNQR 94
Cdd:cd07786 4 AIDQGTTSSRAILFD-HDGNIVAVAQREFTQIYPKPGWVEHDPEEIWESQLAVAR---EALAKAGIRASDIAAIGITNQR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 95 ETTVVWDKLTGEPLYNAVaapvspgssvpvavvpsgspvpaagassVWLDLRTQSTVEKLSKRipGNNNFVKSKTGLPLS 174
Cdd:cd07786 80 ETTVVWDRETGKPVYNAI----------------------------VWQDRRTADICEELKAE--GHEEMIREKTGLVLD 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 175 TYFSAVKLRWLLDNVKKVQEAVEENRALFGTIDSWLIWSLTGGingGVHCTDVTNASRTMLFNIHSLEWDKELCEFFGIP 254
Cdd:cd07786 130 PYFSATKIRWILDNVPGARERAERGELAFGTIDSWLIWKLTGG---KVHATDVTNASRTMLFNIHTLEWDDELLELFGIP 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 255 MEILPNVRSSSEIYGlmkisHSLKAGALEGVPISGCLGDQSAALVGQMCFQDGQAKNTYGTGCFLLCNTGHKCVFSEHGL 334
Cdd:cd07786 207 ASMLPEVKPSSEVFG-----YTDPDLLGAEIPIAGIAGDQQAALFGQACFEPGMAKNTYGTGCFMLMNTGEKPVRSKNGL 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 335 LTTVAYKLGrdKPVYYALEGSVAIAGAVIRWLRDNLGIIKSSEEIEKLAKEVGTSYGCYFVPAFSGLYAPYWEPSARGII 414
Cdd:cd07786 282 LTTIAWQLG--GKVTYALEGSIFIAGAAVQWLRDGLGLIESAAETEALARSVPDNGGVYFVPAFTGLGAPYWDPDARGAI 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 415 CGLTQFTNKCHIAFAALEAVCFQTREILDAMNRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPETTAL--- 491
Cdd:cd07786 360 FGLTRGTTRAHIARAALESIAYQTRDLLEAMEADSGIPLKELRVDGGASANDFLMQFQADILGVPVERPKVTETTALgaa 439
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1958808298 492 -----GAAMAAGAAEGVGVWSLEpedlsavtmERFEPQINAEESEIRYSTWKKAV 541
Cdd:cd07786 440 ylaglAVGLWKSLDELAKLWQVD---------RRFEPSMSEEEREALYAGWKKAV 485
|
|
| ASKHA_NBD_FGGY_GK5-like |
cd07793 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 5 (GK5) and similar proteins; The ... |
15-541 |
1.05e-145 |
|
nucleotide-binding domain (NBD) of metazoan glycerol kinase 5 (GK5) and similar proteins; The subfamily corresponds to a group of metazoan putative glycerol kinases (GK), which may be coded by the GK-like gene, GK5. Sequence comparison shows members of this group are homologs of bacterial GKs, and they retain all functionally important residues. However, GK-like proteins in this family do not have detectable GK activity. The reason remains unclear. It has been suggested that the conserved catalytic residues might facilitate them performing a distinct function. GK5 is a skin-specific kinase expressed predominantly in sebaceous glands. It can form a complex with the sterol regulatory element-binding proteins (SREBPs) through their C-terminal regulatory domains, inhibiting SREBP processing and activation. GK5 also promotes gefitinib resistance by inhibiting apoptosis and cell cycle arrest. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466803 [Multi-domain] Cd Length: 501 Bit Score: 429.29 E-value: 1.05e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 15 AVDQGTSSTRFLVFNSKtAELLSHHQVEIKQEFPREGWVEQDPKEILQSVYECIEKTCEKLGqlnIDISNIKAIGVSNQR 94
Cdd:cd07793 4 AVDVGTTNIRCHIFDKK-GKIIGSSSEKVEVLYPEPGWVEIDPEELWQQFVKVIKEALKNAG---LTPEDIAAIGISTQR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 95 ETTVVWDKLTGEPLYNAVaapvspgssvpvavvpsgspvpaagassVWLDLRTQSTVEKLSK---------------RIP 159
Cdd:cd07793 80 NTFLTWDKKTGKPLHNFI----------------------------TWQDLRAAELCESWNRslllkalrggskflhFLT 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 160 GNNNFVKSKTgLPLSTYFSAVKLRWLLDNVKKVQEAVEENRALFGTIDSWLIWSLTGGingGVHCTDVTNASRTMLFNIH 239
Cdd:cd07793 132 RNKRFLAASV-LKFSTAHVSIRLLWILQNNPELKEAAEKGELLFGTIDTWLLWKLTGG---KVHATDYSNASATGLFDPF 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 240 SLEWDKELCEFFGIPMEILPNVRSSSEIYGLMKISHSLKAgalegVPISGCLGDQSAALVGQMCFQDGQAKNTYGTGCFL 319
Cdd:cd07793 208 TLEWSPILLSLFGIPSSILPEVKDTSGDFGSTDPSIFGAE-----IPITAVVADQQAALFGECCFDKGDVKITMGTGTFI 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 320 LCNTGHKCVFSEHGLLTTVAYKLGrDKPVYyALEGSVAIAGAVIRWLRDNLGIiKSSEEIEKLAKEVGTSYGCYFVPAFS 399
Cdd:cd07793 283 DINTGSKPHASVKGLYPLVGWKIG-GEITY-LAEGNASDTGTVIDWAKSIGLF-DDPSETEDIAESVEDTNGVYFVPAFS 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 400 GLYAPYWEPSARGIICGLTQFTNKCHIAFAALEAVCFQTREILDAMNRDCGIPLSHLQVDGGMTSNKILMQLQADILYIP 479
Cdd:cd07793 360 GLQAPYNDPTACAGFIGLTPSTTKAHLVRAILESIAFRVKQLLETMEKETSIKISSIRVDGGVSNNDFILQLIADLLGKP 439
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958808298 480 VVKPSMPETTalGAAMAAGAAEGVGVWSlEPEDLSAV--TMERFEPQINAEESEIRYSTWKKAV 541
Cdd:cd07793 440 VERPKNTEMS--ALGAAFLAGLASGIWK-SKEELKKLrkIEKIFEPKMDNEKREELYKNWKKAV 500
|
|
| FGGY_N |
pfam00370 |
FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease ... |
12-300 |
1.43e-107 |
|
FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease H-like fold and is structurally related to the C-terminal domain.
Pssm-ID: 395295 [Multi-domain] Cd Length: 245 Bit Score: 322.36 E-value: 1.43e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 12 LVGAVDQGTSSTRFLVFNsKTAELLSHHQVEIKQEFPREGWVEQDPKEILQSVYECIEKTCEklgQLNIDISNIKAIGVS 91
Cdd:pfam00370 1 YYLGIDCGTTSTKAILFN-EQGKIIAVAQLENPQITPHPGWAEQDPDEIWQAVAQCIAKTLS---QLGISLKQIKGIGIS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 92 NQRETTVVWDKLTgEPLYNAVaapvspgssvpvavvpsgspvpaagassVWLDLRTQSTVEKLSKriPGNNNFVKSKTGL 171
Cdd:pfam00370 77 NQGHGTVLLDKND-KPLYNAI----------------------------LWKDRRTAEIVENLKE--EGNNQKLYEITGL 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 172 PLSTYFSAVKLRWLLDNVKKVQEAVEenraLFGTIDSWLIWSLTGginggVHCTDVTNASRTMLFNIHSLEWDKELCEFF 251
Cdd:pfam00370 126 PIWPGFTLSKLRWIKENEPEVFEKIH----KFLTIHDYLRWRLTG-----VFVTDHTNASRSMMFNIHKLDWDPELLAAL 196
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1958808298 252 GIPMEILPNVRSSSEIYGLMKISHSLKAGALEGVPISGCLGDQSAALVG 300
Cdd:pfam00370 197 GIPRDHLPPLVESSEIYGELNPELAAMWGLDEGVPVVGGGGDQQAAAFG 245
|
|
| XylB |
COG1070 |
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ... |
6-489 |
1.26e-91 |
|
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose or hexulose) kinase is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway
Pssm-ID: 440688 [Multi-domain] Cd Length: 494 Bit Score: 290.20 E-value: 1.26e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 6 KAVLGplvgaVDQGTSSTRFLVFNSkTAELLSHHQVEIKQEFPREGWVEQDPKEILQSVYECIEKTCEKLGqlnIDISNI 85
Cdd:COG1070 1 KYVLG-----IDIGTTSVKAVLFDA-DGEVVASASAEYPLSSPHPGWAEQDPEDWWEAVVEAIRELLAKAG---VDPEEI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 86 KAIGVSNQRETTVVWDKlTGEPLYNAVaapvspgssvpvavvpsgspvpaagassVWLDLRTQSTVEKLSKRIPGNNNFv 165
Cdd:COG1070 72 AAIGVSGQMHGLVLLDA-DGEPLRPAI----------------------------LWNDTRAAAEAAELREELGEEALY- 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 166 kSKTGLPLSTYFSAVKLRWLLDNvkkvQEAVEENRALFGTIDSWLIWSLTGginggVHCTDVTNASRTMLFNIHSLEWDK 245
Cdd:COG1070 122 -EITGNPLHPGFTAPKLLWLKEN----EPEIFARIAKVLLPKDYLRYRLTG-----EFVTDYSDASGTGLLDVRTRDWSD 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 246 ELCEFFGIPMEILPNVRSSSEIYGLMKISHSLKAGALEGVPISGCLGDQSAALVGQMCFQDGQAKNTYGTGCFLLCNTGH 325
Cdd:COG1070 192 ELLEALGIDRELLPELVPPGEVAGTLTAEAAAETGLPAGTPVVAGAGDNAAAALGAGAVEPGDAAVSLGTSGVVFVVSDK 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 326 KcVFSEHGLLTTVAYKL-GRdkpvyYALEGSVAIAGAVIRWLRDNLGIIKSS--EEIEKLAKEVGT-SYGCYFVPAFSGL 401
Cdd:COG1070 272 P-LPDPEGRVHTFCHAVpGR-----WLPMGATNNGGSALRWFRDLFADGELDdyEELNALAAEVPPgADGLLFLPYLSGE 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 402 YAPYWEPSARGIICGLTQFTNKCHIAFAALEAVCFQTREILDAMnRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVV 481
Cdd:COG1070 346 RTPHWDPNARGAFFGLTLSHTRAHLARAVLEGVAFALRDGLEAL-EEAGVKIDRIRATGGGARSPLWRQILADVLGRPVE 424
|
....*...
gi 1958808298 482 KPSMPETT 489
Cdd:COG1070 425 VPEAEEGG 432
|
|
| ASKHA_NBD_FGGY |
cd00366 |
nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is ... |
15-489 |
8.26e-88 |
|
nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is predominantly composed of glycerol kinase (GK) and similar carbohydrate kinases including rhamnulokinase (RhuK), xylulokinase (XK), gluconokinase (GntK), ribulokinase (RBK), and fuculokinase (FK). These enzymes catalyze the transfer of a phosphate group, usually from ATP, to their carbohydrate substrates. The monomer of FGGY proteins contains two large domains, which are separated by a deep cleft that forms the active site. One domain is primarily involved in sugar substrate binding, and the other is mainly responsible for ATP binding. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain. Substrate-induced conformational changes and a divalent cation may be required for the catalytic activity. The FGGY family belongs to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466787 [Multi-domain] Cd Length: 392 Bit Score: 276.75 E-value: 8.26e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 15 AVDQGTSSTRFLVFNSkTAELLSHHQVEIKQEFPREGWVEQDPKEILQSVYECIEKTCEKLGqlnIDISNIKAIGVSNQR 94
Cdd:cd00366 4 GIDIGTTSVKAALFDE-DGNLVASASREYPLIYPQPGWAEQDPEDWWQAVVEAIREVLAKAG---IDPSDIAAIGISGQM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 95 ETTVVWDKlTGEPLYNAVaapvspgssvpvavvpsgspvpaagassVWLDlrtqstveklskripgnnnfvksktglpls 174
Cdd:cd00366 80 PGVVLVDA-DGNPLRPAI----------------------------IWLD------------------------------ 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 175 tyfsavklrwlldnvkkvqeaveeNRALFGTIDSWLIWSLTGginggVHCTDVTNASRTMLFNIHSLEWDKELCEFFGIP 254
Cdd:cd00366 101 ------------------------RRAKFLQPNDYIVFRLTG-----EFAIDYSNASGTGLYDIKTGDWSEELLDALGIP 151
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 255 MEILPNVRSSSEIYGlmKISH--SLKAGALEGVPISGCLGDQSAALVGQMCFQDGQAKNTYGTGCFLLCNTGhKCVFSEH 332
Cdd:cd00366 152 REKLPPIVESGEVVG--RVTPeaAEETGLPAGTPVVAGGGDTAAAALGAGVVEPGDAVDSTGTSSVLSVCTD-EPVPPDP 228
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 333 GLLTTVAYKLGRdkpvyYALEGSVAIAGAVIRWLRDNLGIIKSSEE----IEKLAKEVGT-SYGCYFVPAFSGLYAPYWE 407
Cdd:cd00366 229 RLLNRCHVVPGL-----WLLEGAINTGGASLRWFRDEFGEEEDSDAeyegLDELAAEVPPgSDGLIFLPYLSGERSPIWD 303
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 408 PSARGIICGLTQFTNKCHIAFAALEAVCFQTREILDAMnRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPE 487
Cdd:cd00366 304 PAARGVFFGLTLSHTRAHLIRAVLEGVAYALRDNLEIL-EELGVKIKEIRVTGGGAKSRLWNQIKADVLGVPVVVPEVAE 382
|
..
gi 1958808298 488 TT 489
Cdd:cd00366 383 GA 384
|
|
| ASKHA_NBD_FGGY_YgcE-like |
cd07779 |
nucleotide-binding domain (NBD) of Escherichia coli sugar kinase YgcE and similar proteins; ... |
15-489 |
1.86e-87 |
|
nucleotide-binding domain (NBD) of Escherichia coli sugar kinase YgcE and similar proteins; This subfamily contains a group of uncharacterized proteins with similarity to Escherichia coli sugar kinase YgcE. They belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466798 [Multi-domain] Cd Length: 433 Bit Score: 277.09 E-value: 1.86e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 15 AVDQGTSSTRFLVFNsKTAELLSHHQVEIKQEFPREGWVEQDPKEILQSVYECIEKTCEKLGqlnIDISNIKAIGVSNQR 94
Cdd:cd07779 4 GIDVGTTSTRAIIFD-LDGNIVASGYREYPPYYPEPGWVEQDPDDWWDALCEALKEAVAKAG---VDPEDIAAIGLTSQR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 95 ETTVVWDKlTGEPLYNAVaapvspgssvpvavvpsgspvpaagassVWLDLRTqstveklskripgnnnfvksktglpls 174
Cdd:cd07779 80 STFVPVDE-DGRPLRPAI----------------------------SWQDKRT--------------------------- 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 175 tyfsavklrwlldnvkkvqeaveenrALFGTIDSWLIWSLTggingGVHCTDVTNASRTMLFNIHSLEWDKELCEFFGIP 254
Cdd:cd07779 104 --------------------------AKFLTVQDYLLYRLT-----GEFVTDTTSASRTGLPDIRTRDWSDDLLDAFGID 152
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 255 MEILPNVRSSSEIYGlmKISH--SLKAGALEGVPISGCLGDQSAALVGQMCFQDGQAKNTYGTGCFLLCNTgHKCVFSEH 332
Cdd:cd07779 153 RDKLPELVPPGTVIG--TLTKeaAEETGLPEGTPVVAGGGDQQCAALGAGVLEPGTASLSLGTAAVVIAVS-DKPVEDPE 229
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 333 GLLTTVAYKLgrdkPVYYALEGSVAIAGAVIRWLRDNLG--------IIKSSEE-IEKLAKEVGT-SYGCYFVPAFSGLY 402
Cdd:cd07779 230 RRIPCNPSAV----PGKWVLEGSINTGGSAVRWFRDEFGqdevaekeLGVSPYElLNEEAAKSPPgSDGLLFLPYLAGAG 305
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 403 APYWEPSARGIICGLTQFTNKCHIAFAALEAVCFQTREILDAMnRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVK 482
Cdd:cd07779 306 TPYWNPEARGAFIGLTLSHTRAHLARAILEGIAFELRDNLEAM-EKAGVPIEEIRVSGGGSKSDLWNQIIADVFGRPVER 384
|
....*..
gi 1958808298 483 PSMPETT 489
Cdd:cd07779 385 PETSEAT 391
|
|
| ASKHA_NBD_FGGY_FK |
cd07773 |
nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), ... |
12-489 |
3.09e-78 |
|
nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), also called L-fuculose kinase, catalyzes the ATP-dependent phosphorylation of L-fuculose to produce L-fuculose-1-phosphate and ADP. It can also phosphorylate, with lower efficiency, D-ribulose, D-xylulose and D-fructose. The presence of Mg2+ or Mn2+ is required for enzymatic activity. FKs belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466793 [Multi-domain] Cd Length: 443 Bit Score: 253.66 E-value: 3.09e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 12 LVGaVDQGTSSTRFLVFNsKTAELLSHHQVEIKQEFPREGWVEQDPKEILQSVYECIEKTCEKLGQlnidiSNIKAIGVS 91
Cdd:cd07773 2 LLG-IDIGTTNVKAVLFD-EDGRILASASRETPLIHPGPGWAELDPEELWEAVKEAIREAAAQAGP-----DPIAAISVS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 92 NQRETTVVWDKlTGEPLYNAVaapvspgssvpvavvpsgspvpaagassVWLDLRTQSTVEKLSKRIPGNNNFvkSKTGL 171
Cdd:cd07773 75 SQGESGVPVDR-DGEPLGPAI----------------------------VWFDPRGKEEAEELAERIGAEELY--RITGL 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 172 PLSTYFSAVKLRWLLDNVKKVQEAVeenrALFGTIDSWLIWSLTGginggVHCTDVTNASRTMLFNIHSLEWDKELCEFF 251
Cdd:cd07773 124 PPSPMYSLAKLLWLREHEPEIFAKA----AKWLSVADYIAYRLTG-----EPVTDYSLASRTMLFDIRKRTWSEELLEAA 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 252 GIPMEILPNVRSSSEIYGLMKISHSLKAGALEGVPIsgCLG--DQSAALVGQMCFQDGQAKNTYGTG-CFLLC-NTGHKC 327
Cdd:cd07773 195 GIDASLLPELVPSGTVIGTVTPEAAEELGLPAGTPV--VVGghDHLCAALGAGVIEPGDVLDSTGTAeALLAVvDEPPLD 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 328 VFSEHGLLTTVAYKLGRdkpvYYALEGSVAiAGAVIRWLRDNLGI--IKSSEEIEKLAKEVGTSYGCYFVPAFSGLYAPY 405
Cdd:cd07773 273 EMLAEGGLSYGHHVPGG----YYYLAGSLP-GGALLEWFRDLFGGdeSDLAAADELAEAAPPGPTGLLFLPHLSGSGTPD 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 406 WEPSARGIICGLTQFTNKCHIAFAALEAVCFQTREILDAMnRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSM 485
Cdd:cd07773 348 FDPDARGAFLGLTLGTTRADLLRAILEGLAFELRLNLEAL-EKAGIPIDEIRAVGGGARSPLWLQLKADILGRPIEVPEV 426
|
....
gi 1958808298 486 PETT 489
Cdd:cd07773 427 PEAT 430
|
|
| ASKHA_NBD_FGGY_EcXK-like |
cd07808 |
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar ... |
8-489 |
1.72e-75 |
|
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar proteins; The subfamily contains a group of uncharacterized proteins with similarity to Escherichia coli xylulose kinase (EcXK). XK (EC 2.7.1.17), also called xylulokinase or D-xylulose kinase, catalyze the rate-limiting step in the ATP-dependent phosphorylation of D-xylulose to produce D-xylulose 5-phosphate (X5P), a molecule that may play an important role in the regulation of glucose metabolism and lipogenesis. EcXK, also known as 1-deoxy-D-xylulokinase, can also catalyze the phosphorylation of 1-deoxy-D-xylulose to 1-deoxy-D-xylulose 5-phosphate, with lower efficiency. It can also use D-ribulose, xylitol and D-arabitol, but D-xylulose is preferred over the other substrates. EcXK has a weak substrate-independent Mg-ATP-hydrolyzing activity. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466808 [Multi-domain] Cd Length: 482 Bit Score: 247.45 E-value: 1.72e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 8 VLGplvgaVDQGTSSTRFLVFNSKtAELLSHHQVEIKQEFPREGWVEQDPKEILQSVYECIEKTcekLGQLNIDISNIKA 87
Cdd:cd07808 2 LLG-----IDLGTSSVKAVLVDED-GRVLASASAEYPTSSPKPGWAEQDPEDWWQATKEALREL---LAKAGISPSDIAA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 88 IGVSNQRETTVVWDKlTGEPLYNAVaapvspgssvpvavvpsgspvpaagassVWLDLRTQSTVEKLSKRIPgnnNFVKS 167
Cdd:cd07808 73 IGLTGQMHGLVLLDK-NGRPLRPAI----------------------------LWNDQRSAAECEELEARLG---DEILI 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 168 KTGLPLSTYFSAVKLRWLL----DNVKKVqeaveenRALFGTIDsWLIWSLTGginggVHCTDVTNASRTMLFNIHSLEW 243
Cdd:cd07808 121 ITGNPPLPGFTLPKLLWLKenepEIFARI-------RKILLPKD-YLRYRLTG-----ELATDPSDASGTLLFDVEKREW 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 244 DKELCEFFGIPMEILPNVRSSSEIYGlmKISHSLkAGAL---EGVP-ISGClGDQSAALVGQMCFQDGQAKNTYGTGCFL 319
Cdd:cd07808 188 SEELLEALGLDPSILPPIVESTEIVG--TLTPEA-AEELglpEGTPvVAGA-GDNAAAALGAGVVEPGDALISLGTSGVV 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 320 LCNTgHKCVFSEHGLLTTVAYKLGrdkPVYYALeGSVAIAGAVIRWLRDNLGIIKSS-EEIEKLAKEVG-TSYGCYFVPA 397
Cdd:cd07808 264 FAPT-DKPVPDPKGRLHTFPHAVP---GKWYAM-GVTLSAGLSLRWLRDLFGPDRESfDELDAEAAKVPpGSEGLLFLPY 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 398 FSGLYAPYWEPSARGIICGLTQFTNKCHIAFAALEAVCFQTREILDAMnRDCGIPLSHLQVDGGMTSNKILMQLQADILY 477
Cdd:cd07808 339 LSGERTPYWDPNARGSFFGLSLSHTRAHLARAVLEGVAFSLRDSLEVL-KELGIKVKEIRLIGGGAKSPLWRQILADVLG 417
|
490
....*....|..
gi 1958808298 478 IPVVKPSMPETT 489
Cdd:cd07808 418 VPVVVPAEEEGS 429
|
|
| ASKHA_NBD_FGGY_GntK |
cd07770 |
nucleotide-binding domain (NBD) of gluconate kinase (GntK) and similar proteins; GntK (EC 2.7. ... |
15-489 |
4.05e-72 |
|
nucleotide-binding domain (NBD) of gluconate kinase (GntK) and similar proteins; GntK (EC 2.7.1.12), also known as gluconokinase, catalyzes the ATP-dependent phosphorylation of D-gluconate and produce 6-phospho-D-gluconate and ADP. The presence of Mg2+ might be required for catalytic activity. The prototypical member of this subfamily is GntK from Lactobacillus acidophilus. Unlike Escherichia coli GntK, which belongs to the superfamily of P-loop containing nucleoside triphosphate hydrolases, Members of this subfamily are homologous to glycerol kinase, xylulose kinase, and rhamnulokinase from Escherichia coli. They have been classified as members of the FGGY family of carbohydrate kinases, which contain two large domains separated by a deep cleft that forms the active site. This model spans both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466790 [Multi-domain] Cd Length: 478 Bit Score: 238.61 E-value: 4.05e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 15 AVDQGTSSTRFLVFNSKtAELLSHHQVEIKQEFPREGWVEQDPKEILQSVYECIEKTCEKLGQLNIDisnikAIGVSNQR 94
Cdd:cd07770 4 GIDIGTTSTKAVLFDED-GRVVASSSAEYPLIRPEPGWAEQDPEEILEAVLEALKEVLAKLGGGEVD-----AIGFSSAM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 95 ETTVVWDKlTGEPLynavaAPVSPgssvpvavvpsgspvpaagassvWLDLRTQSTVEKLSKRIPGNNnfVKSKTGLPLS 174
Cdd:cd07770 78 HSLLGVDE-DGEPL-----TPVIT-----------------------WADTRAAEEAERLRKEGDGSE--LYRRTGCPIH 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 175 TYFSAVKLRWLldnvKKVQEAVEENRALFGTIDSWLIWSLTGginggVHCTDVTNASRTMLFNIHSLEWDKELCEFFGIP 254
Cdd:cd07770 127 PMYPLAKLLWL----KEERPELFAKAAKFVSIKEYLLYRLTG-----ELVTDYSTASGTGLLNIHTLDWDEEALELLGID 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 255 MEILPNVRSSSEIYGLMKISHSLKAGALEGVPISGCLGDQSAALVGQMCFQDGQAKNTYGTgcfllcnTGHKCVFSEHGL 334
Cdd:cd07770 198 EEQLPELVDPTEVLPGLKPEFAERLGLLAGTPVVLGASDGALANLGSGALDPGRAALTVGT-------SGAIRVVSDRPV 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 335 LT----TVAYKLGRDKPVyyaLEGSVAIAGAVIRWLRDNLGIIKSS-EEIEKLAKEVG-TSYGCYFVPAFSGLYAPYWEP 408
Cdd:cd07770 271 LDppgrLWCYRLDENRWL---VGGAINNGGNVLDWLRDTLLLSGDDyEELDKLAEAVPpGSHGLIFLPYLAGERAPGWNP 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 409 SARGIICGLTQFTNKCHIAFAALEAVCFQTREILDAMnRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPET 488
Cdd:cd07770 348 DARGAFFGLTLNHTRADILRAVLEGVAFNLKSIYEAL-EELAGPVKEIRASGGFLRSPLWLQILADVLGRPVLVPEEEEA 426
|
.
gi 1958808298 489 T 489
Cdd:cd07770 427 S 427
|
|
| ASKHA_NBD_FGGY_RrXK-like |
cd07804 |
nucleotide-binding domain (NBD) of Rhodospirillum rubrum xylulose kinase (RrXK) and similar ... |
12-484 |
4.05e-65 |
|
nucleotide-binding domain (NBD) of Rhodospirillum rubrum xylulose kinase (RrXK) and similar proteins; The subfamily contains a group of uncharacterized proteins with similarity to Rhodospirillum rubrum xylulose kinase (RrXK). Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466806 [Multi-domain] Cd Length: 451 Bit Score: 219.32 E-value: 4.05e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 12 LVGaVDQGTSSTRFLVFNSKtAELLSHHQVEIKQEFPREGWVEQDPKEILQSVYECIEKTCEKLGqlnIDISNIKAIGVS 91
Cdd:cd07804 2 LLG-IDIGTTGTKGVLVDED-GKVLASASIEHDLLTPKPGWAEHDPEVWWGAVCEIIRELLAKAG---ISPKEIAAIGVS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 92 NQRETTVVWDKlTGEPLYNAVaapvspgssvpvavvpsgspvpaagassVWLDLRTQSTVEKLSKRIPGNNNFvkSKTGL 171
Cdd:cd07804 77 GLVPALVPVDE-NGKPLRPAI----------------------------LYGDRRATEEIEWLNENIGEDRIF--EITGN 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 172 PLSTYFSAVKLRWLLDNvkkvQEAVEENRALFGTIDSWLIWSLTGginggVHCTDVTNASRTM-LFNIHSLEWDKELCEF 250
Cdd:cd07804 126 PLDSQSVGPKLLWIKRN----EPEVFKKTRKFLGAYDYIVYKLTG-----EYVIDYSSAGNEGgLFDIRKRTWDEELLEA 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 251 FGIPMEILPNVRSSSEIYGlmKISH--SLKAGALEGVPISGCLGDQSAALVGQMCFQDGQAKNTYGT-GCFLLCntgHKC 327
Cdd:cd07804 197 LGIDPDLLPELVPSTEIVG--EVTKeaAEETGLAEGTPVVAGTVDAAASALSAGVVEPGDLLLMLGTaGDIGVV---TDK 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 328 VFSEHGLLTTVAyklgrDKPVYYALEGSVAIAGAVIRWLRDNLGIIKSSEE----------IEKLAKEVG-TSYGCYFVP 396
Cdd:cd07804 272 LPTDPRLWLDYH-----DIPGTYVLNGGMATSGSLLRWFRDEFAGEEVEAEksggdsaydlLDEEAEKIPpGSDGLIVLP 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 397 AFSGLYAPYWEPSARGIICGLTQFTNKCHIAFAALEAVCFQTREILDAMNRDcGIPLSHLQVDGGMTSNKILMQLQADIL 476
Cdd:cd07804 347 YFMGERTPIWDPDARGVIFGLTLSHTRAHLYRALLEGVAYGLRHHLEVIREA-GLPIKRLVAVGGGAKSPLWRQIVADVT 425
|
....*...
gi 1958808298 477 YIPVVKPS 484
Cdd:cd07804 426 GVPQEYVK 433
|
|
| ASKHA_NBD_FGGY_CvXK-like |
cd07805 |
nucleotide-binding domain (NBD) of Chromobacterium violaceum xylulose kinase (CvXK) and ... |
15-487 |
1.02e-62 |
|
nucleotide-binding domain (NBD) of Chromobacterium violaceum xylulose kinase (CvXK) and similar proteins; The subfamily contains a group of uncharacterized proteins with similarity to Chromobacterium violaceum xylulose kinase (CvXK). Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466807 [Multi-domain] Cd Length: 485 Bit Score: 213.92 E-value: 1.02e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 15 AVDQGTSSTrflvfnsKTA------ELLSHHQVEIKQEFPREGWVEQDPKEILQSVYECiekTCEKLGQLNIDISNIKAI 88
Cdd:cd07805 4 AIDLGTSGV-------KAAlvdldgELVASAFAPYPTYYPKPGWAEQDPEDWWDAVCRA---TRALLEKSGIDPSDIAAI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 89 GVSNQRETTVVWDKlTGEPLYNAVaapvspgssvpvavvpsgspvpaagassVWLDLRTQSTVEKLSKRIPGNNnFVKSK 168
Cdd:cd07805 74 AFSGQMQGVVPVDK-DGNPLRNAI----------------------------IWSDTRAAEEAEEIAGGLGGIE-GYRLG 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 169 TGLPLSTYFSAVKLRWLLDNVKkvqEAVEENRALFGTIDsWLIWSLTGginggVHCTDVTNASRTMLFNIHSLEWDKELC 248
Cdd:cd07805 124 GGNPPSGKDPLAKILWLKENEP---EIYAKTHKFLDAKD-YLNFRLTG-----RAATDPSTASTTGLMDLRKRRWSEELL 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 249 EFFGIPMEILPNVRSSSEIYG--LMKISHSLkaGALEGVPISGCLGDQSAALVGQMCFQDGQAkNTY-GTGCFLLCNTGH 325
Cdd:cd07805 195 RAAGIDPDKLPELVPSTEVVGelTPEAAAEL--GLPAGTPVVGGGGDAAAAALGAGAVEEGDA-HIYlGTSGWVAAHVPK 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 326 KCVFSEHGlLTTVAYKLgrdkPVYYALEGSVAIAGAVIRWLRDNLGIIKSS-----EEIEKLAKEVGT-SYGCYFVPAFS 399
Cdd:cd07805 272 PKTDPDHG-IFTLASAD----PGRYLLAAEQETAGGALEWARDNLGGDEDLgaddyELLDELAAEAPPgSNGLLFLPWLN 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 400 GLYAPYWEPSARGIICGLTQFTNKCHIAFAALEAVCFQTREILDAMNRDCGiPLSHLQVDGGMTSNKILMQLQADILYIP 479
Cdd:cd07805 347 GERSPVEDPNARGAFIGLSLEHTRADLARAVLEGVAFNLRWLLEALEKLTR-KIDELRLVGGGARSDLWCQILADVLGRP 425
|
....*...
gi 1958808298 480 VVKPSMPE 487
Cdd:cd07805 426 VEVPENPQ 433
|
|
| FGGY_C |
pfam02782 |
FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease ... |
309-492 |
6.62e-46 |
|
FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease H-like fold and is structurally related to the N-terminal domain.
Pssm-ID: 426979 [Multi-domain] Cd Length: 197 Bit Score: 160.18 E-value: 6.62e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 309 AKNTYGTGCFLLCNTGHKCVFsEHGLLTTVAyklGRDKPVYYALEGSVAIAGAVIRWLRDNLGI---------IKSSEEI 379
Cdd:pfam02782 1 LAISAGTSSFVLVETPEPVLS-VHGVWGPYT---NEMLPGYWGLEGGQSAAGSLLAWLLQFHGLreelrdagnVESLAEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 380 EKLAKEVGTSyGCYFVPAFSGLYAPYWEPSARGIICGLTQFTNKCHIAFAALEAVCFQTREILDAMNRDCGIPLSHLQVD 459
Cdd:pfam02782 77 AALAAVAPAG-GLLFYPDFSGNRAPGADPGARGSITGLSSPTTLAHLYRAILESLALQLRQILEALTKQEGHPIDTIHVS 155
|
170 180 190
....*....|....*....|....*....|...
gi 1958808298 460 GGMTSNKILMQLQADILYIPVVKPSMPETTALG 492
Cdd:pfam02782 156 GGGSRNPLLLQLLADALGLPVVVPGPDEATALG 188
|
|
| ASKHA_NBD_FGGY_EcLyxK-like |
cd07802 |
nucleotide-binding domain (NBD) of Escherichia coli L-xylulose/3-keto-L-gulonate kinase ... |
12-489 |
1.01e-44 |
|
nucleotide-binding domain (NBD) of Escherichia coli L-xylulose/3-keto-L-gulonate kinase (EcLyxK) and similar proteins; The subfamily contains a group of uncharacterized proteins with similarity to Escherichia coli L-xylulose/3-keto-L-gulonate kinase (EcLyxK; EC 2.7.1.-/EC 2.7.1.53), Pasteurella multocida L-xylulose kinase (PmLyX, also known as L-xylulokinase; EC 2.7.1.53), and Brucella abortus erythritol kinase (BaEryA; EC 2.7.1.215). EcLyxK catalyzes the phosphorylation of L-xylulose and 3-keto-L-gulonate. It is involved in L-lyxose utilization via xylulose and may also be involved in the utilization of 2,3-diketo-L-gulonate. PmLyX catalyzes the phosphorylation of L-xylulose only. BaEryA catalyzes the phosphorylation of erythritol to D-erythritol-1-phosphate. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466805 [Multi-domain] Cd Length: 444 Bit Score: 164.26 E-value: 1.01e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 12 LVGaVDQGTSSTRFLVFNSKTAELLSHHqVEIKQEFPREGWVEQDPKEILQSVYECIEKTCEKLGqlnIDISNIKAIGVS 91
Cdd:cd07802 2 LLG-IDNGTTNVKAVLFDLDGREIAVAS-RPTPVISPRPGWAERDMDELWQATAEAIRELLEKSG---VDPSDIAGVGVT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 92 NQRETTVVWDKlTGEPLYNAVaapvspgssvpvavvpsgspvpaagassVWLDLRTQSTVEKLSKRipGNNNFVKSKTGL 171
Cdd:cd07802 77 GHGNGLYLVDK-DGKPVRNAI----------------------------LSNDSRAADIVDRWEED--GTLEKVYPLTGQ 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 172 PLSTYFSAVKLRWLLDNVKKVQEAVeenRALFGTIDsWLIWSLTggingGVHCTDVTNASrTMLFNIHSLEWDKELCEFF 251
Cdd:cd07802 126 PLWPGQPVALLRWLKENEPERYDRI---RTVLFCKD-WIRYRLT-----GEISTDYTDAG-SSLLDLDTGEYDDELLDLL 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 252 GIP--MEILPNVRSSSEIYGLMKISHSLKAGALEGVPISGCLGDQSAALVGQMCFQDGQAKNTYGTGCfllCNTG--HKC 327
Cdd:cd07802 196 GIEelKDKLPPLVPSTEIAGRVTAEAAALTGLPEGTPVAAGAFDVVASALGAGAVDEGQLCVILGTWS---INEVvtDEP 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 328 VFSEHGLLTTvaykLGRDKPVYYALEGSVAIAGaVIRWLRDNLG------IIKSSEEIEKLAKEVG-TSYGCYFVPaFsg 400
Cdd:cd07802 273 VVPDSVGSNS----LHADPGLYLIVEASPTSAS-NLDWFLDTLLgeekeaGGSDYDELDELIAAVPpGSSGVIFLP-Y-- 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 401 LYAPYWEPSARGIICGLTQFTNKCHIAFAALEAVCFQTREILDAMNRDCgiPLSHLQVDGGMTSNKILMQLQADILYIPV 480
Cdd:cd07802 345 LYGSGANPNARGGFFGLTAWHTRAHLLRAVYEGIAFSHRDHLERLLVAR--KPETIRLTGGGARSPVWAQIFADVLGLPV 422
|
....*....
gi 1958808298 481 VKPSMPETT 489
Cdd:cd07802 423 EVPDGEELG 431
|
|
| ASKHA_NBD_FGGY_YoaC-like |
cd07798 |
nucleotide-binding domain (NBD) of Bacillus subtilis sugar kinase YoaC and similar proteins; ... |
15-489 |
1.30e-42 |
|
nucleotide-binding domain (NBD) of Bacillus subtilis sugar kinase YoaC and similar proteins; The subfamily includes a group of uncharacterized proteins with similarity to Bacillus subtilis sugar kinase YoaC. It is part of the yoaDCB operon and induced by sulfate. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466804 [Multi-domain] Cd Length: 448 Bit Score: 158.54 E-value: 1.30e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 15 AVDQGTSSTRFLVFNSKTAELLSHHQVEIKQEFPREGW-VEQDPKEILQSVYECIEKTcekLGQLNIDISNIKAIGVSNQ 93
Cdd:cd07798 4 VIDIGTGGGRCALVDSEGKIVAIAYREWEYYTDDDYPDaKEFDPEELWEKICEAIREA---LKKAGISPEDISAVSSTSQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 94 RETTVVWDKlTGEPLYnavaapvspgssvpvaVVPSgspvpaagassvwLDLRTqstvEKLSKRIPGNNNFVKSK-TGLP 172
Cdd:cd07798 81 REGIVFLDK-DGRELY----------------AGPN-------------IDARG----VEEAAEIDDEFGEEIYTtTGHW 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 173 LSTYFSAVKLRWLldnvKKVQEAVEENRALFGTIDSWLIWSLTGGInggvhCTDVTNASRTMLFNIHSLEWDKELCEFFG 252
Cdd:cd07798 127 PTELFPAARLLWF----KENRPEIFERIATVLSISDWIGYRLTGEL-----VSEPSQASETQLFDIKKREWSQELLEALG 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 253 IPMEILPNVRSSSEIYGlmKISHSLKA--GALEGVPISGCLGDQSAALVGQMCFQDGQAKNTYGTGCFLLCNTGhKCVFS 330
Cdd:cd07798 198 LPPEILPEIVPSGTVLG--TVSEEAARelGLPEGTPVVVGGADTQCALLGSGAIEPGDIGIVAGTTTPVQMVTD-EPIID 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 331 EHGLLTTVAYkLGRDKpvyYALEGSVAIAGAVIRWLRDNL--GIIKSSEEIEKLAKEVG-TSYGCYfvpAFSGLYAPYwe 407
Cdd:cd07798 275 PERRLWTGCH-LVPGK---WVLESNAGVTGLNYQWLKELLygDPEDSYEVLEEEASEIPpGANGVL---AFLGPQIFD-- 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 408 PSARGIICGLTQFT--------NKCHIAFAALEAVCFQTREILDAMNRDCGIPLSHLQVDGGMTSNKILMQLQADILYIP 479
Cdd:cd07798 346 ARLSGLKNGGFLFPtplsaselTRGDFARAILENIAFAIRANLEQLEEVSGREIPYIILCGGGSRSALLCQILADVLGKP 425
|
490
....*....|
gi 1958808298 480 VVKPSMPETT 489
Cdd:cd07798 426 VLVPEGREAS 435
|
|
| ASKHA_NBD_FGGY_SePSK_AtXK1-like |
cd07783 |
nucleotide-binding domain (NBD) of Synechococcus elongatus putative sugar kinase (SePSK), ... |
15-488 |
1.45e-42 |
|
nucleotide-binding domain (NBD) of Synechococcus elongatus putative sugar kinase (SePSK), Arabidopsis thaliana xylulose kinase-1 (AtXK-1) and similar proteins; This subfamily corresponds to a group of uncharacterized bacterial proteins with similarity to Synechococcus elongatus putative sugar kinase (also known as SePSK; D-ribulose kinase; D-ribulokinase) and Arabidopsis thaliana xylulose kinase-1 (also known as AtXK-1; D-ribulose kinase; D-ribulokinase; inactive xylulose kinase 1). Both kinases exhibit ATP hydrolysis without substrate and can phosphorylate D-ribulose. They belong to the ribulokinase-like carbohydrate kinases, a subfamily of FGGY family carbohydrate kinases. Ribulokinase-like carbohydrate kinases are responsible for the phosphorylation of sugars such as L-ribulose and D-ribulose. Their monomers contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466801 [Multi-domain] Cd Length: 429 Bit Score: 157.77 E-value: 1.45e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 15 AVDQGTSSTRFLVFNSKtAELLSHHQVEIKQEFPREGWVEQDPKEILQSVYECIEKTCEKLgqlniDISNIKAIGVSNQR 94
Cdd:cd07783 4 GIDLGTSGVRAVVVDED-GTVLASASEPYPTSRPGPGWVEQDPEDWWEALRSLLRELPAEL-----RPRRVVAIAVDGTS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 95 ETTVVWDKlTGEPLYNAVaapvspgssvpvavvpsgspvpaagassVWLDLRTQSTVEKLSKRIPgnnnFVKSKTGLPLS 174
Cdd:cd07783 78 GTLVLVDR-EGEPLRPAI----------------------------MYNDARAVAEAEELAEAAG----AVAPRTGLAVS 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 175 TYFSAVKLRWLLDNVKKVQEAVeenrALFGTIDSWLIWSLTGGinggVHCTDVTNASRTmLFNIHSLEWDKELCEFFGIP 254
Cdd:cd07783 125 PSSSLAKLLWLKRHEPEVLAKT----AKFLHQADWLAGRLTGD----RGVTDYNNALKL-GYDPETGRWPSWLLALLGIP 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 255 MEILPNVRSSSEIYG--LMKISHSLkaGALEGVPIsgCLG--DQSAALVGQMCFQDGQAKNTYGTgcfllcntghkcvfs 330
Cdd:cd07783 196 PDLLPRVVAPGTVIGtlTAEAAEEL--GLPAGTPV--VAGttDSIAAFLASGAVRPGDAVTSLGT--------------- 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 331 ehglltTVAYKLGRDKPV---------------YYALEGSVAIAGAVIRWLrdnlgiiKSSEEIEKLAKEVGTSY--GCY 393
Cdd:cd07783 257 ------TLVLKLLSDKRVpdpgggvyshrhgdgYWLVGGASNTGGAVLRWF-------FSDDELAELSAQADPPGpsGLI 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 394 FVP-AFSGLYAPYWEPSARGIICGLTqfTNKCHIAFAALEAVCFQTREILDAMNRDCGIPLSHLQVDGGMTSNKILMQLQ 472
Cdd:cd07783 324 YYPlPLRGERFPFWDPDARGFLLPRP--HDRAEFLRALLEGIAFIERLGYERLEELGAPPVEEVRTAGGGARNDLWNQIR 401
|
490
....*....|....*.
gi 1958808298 473 ADILYIPVVKPSMPET 488
Cdd:cd07783 402 ADVLGVPVVIAEEEEA 417
|
|
| ASKHA_NBD_FGGY_BaXK-like |
cd07809 |
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and ... |
8-488 |
2.47e-34 |
|
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and similar proteins; The subfamily includes a group of uncharacterized proteins with similarity to xylulose kinases (XKs) from Bifidobacterium adolescentis, Streptomyces coelicolor, Actinoplanes missouriensis and Haemophilus influenzae. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466809 [Multi-domain] Cd Length: 443 Bit Score: 134.99 E-value: 2.47e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 8 VLGplvgaVDQGTSSTRFLVFNSKTAELLSHHQVEIKQEFPREGWVEQDPKEILQSVYECIEKTcekLGQLNIDISNIKA 87
Cdd:cd07809 2 VLG-----IDLGTQSIKAVLIDAETGRVVASGSAPHENILIDPGWAEQDPEDWWDALQAAFAQL---LKDAGAELRDVAA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 88 IGVSNQRETTVVWDKlTGEPLYNAVaapvspgssvpvavvpsgspvpaagassVWLDLRTQSTVEKLSKRIPGNNnfvKS 167
Cdd:cd07809 74 IGISGQMHGLVALDA-DGKVLRPAK----------------------------LWCDTRTAPEAEELTEALGGKK---CL 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 168 KTGLPLSTYFSAVKLRWLLDN----VKKVqeaveenrALFGTIDSWLIWSLTGGinggvHCTDVTNASRTMLFNIHSLEW 243
Cdd:cd07809 122 LVGLNIPARFTASKLLWLKENepehYARI--------AKILLPHDYLNWKLTGE-----KVTGLGDASGTFPIDPRTRDY 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 244 DKELCEFF---GIPMEILPNVRSSSEIYGLMKISHSLKAGALEGVPISGCLGDQSAALVGQMCFQDGQAKNTYGT-GCfl 319
Cdd:cd07809 189 DAELLAAIdpsRDLRDLLPEVLPAGEVAGRLTPEGAEELGLPAGIPVAPGEGDNMTGALGTGVVNPGTVAVSLGTsGT-- 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 320 LCNTGHKCVFSEHGLLTTVAyklgrDKPVYYALegSVAIAGAVIRWLRDNLGIIKSS-EEIEKLAKEV-GTSYGCYFVPA 397
Cdd:cd07809 267 AYGVSDKPVSDPHGRVATFC-----DSTGGMLP--LINTTNCLTAWTELFRELLGVSyEELDELAAQApPGAGGLLLLPF 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 398 FSGLYAPYWePSARGIICGLTQF-TNKCHIAFAALEAVCFQTREILDAMnRDCGIPLSHLQVDGGMTSNKILMQLQADIL 476
Cdd:cd07809 340 LNGERTPNL-PHGRASLVGLTLSnFTRANLARAALEGATFGLRYGLDIL-RELGVEIDEIRLIGGGSKSPVWRQILADVF 417
|
490
....*....|..
gi 1958808298 477 YIPVVKPSMPET 488
Cdd:cd07809 418 GVPVVVPETGEG 429
|
|
| ASKHA_NBD_FGGY_BaEryA-like |
cd24121 |
nucleotide-binding domain (NBD) of Brucella abortus erythritol kinase (BaEryA) and similar ... |
12-488 |
2.25e-28 |
|
nucleotide-binding domain (NBD) of Brucella abortus erythritol kinase (BaEryA) and similar proteins; The subfamily contains a group of uncharacterized proteins with similarity to Brucella abortus erythritol kinase (BaEryA; EC 2.7.1.215). It catalyzes the phosphorylation of erythritol to D-erythritol-1-phosphate. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466971 [Multi-domain] Cd Length: 452 Bit Score: 118.11 E-value: 2.25e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 12 LVGaVDQGTSSTRFLVFNSKTAELlSHHQVEIKQEFPREGWVEQDPKEILQSVYECIEKTCEKLGQLNidiSNIKAIGVS 91
Cdd:cd24121 2 LIG-IDAGTSVVKAVAFDLDGREL-AVAARRNAVLYPQPGWAEQDMNETWQAVVATIREVVAKLDVLP---DRVAAIGVT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 92 NQRETTvvWdkLTGEplynavaapvspgssvpvavvpSGSPV-PAAgassVWLDLRTQSTVEKLSKRipGNNNFVKSKTG 170
Cdd:cd24121 77 GQGDGT--W--LVDE----------------------DGRPVrDAI----LWLDGRAADIVERWQAD--GIAEAVFEITG 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 171 LPLSTYFSAVKLRWLLDNVKkvqEAVEENRALFGTIDsWLIWSLTGGInggvhCTDVTNASRTMlFNIHSLEWDKELCEF 250
Cdd:cd24121 125 TGLFPGSQAAQLAWLKENEP---ERLERARTALHCKD-WLFYKLTGEI-----ATDPSDASLTF-LDFRTRQYDDEVLDL 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 251 FGIP--MEILPNVRSSSEIYGLMKISHSLKAGALEGVPISGCLGDQSAALVGQMCFQDGQAKNTYGTGCFllcntghkcv 328
Cdd:cd24121 195 LGLEelRHLLPPIRPGTEVIGPLTPEAAAATGLPAGTPVVLGPFDVVATALGSGAIEPGDACSILGTTGV---------- 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 329 fseHGLLTTVAYkLGRDKP---VYYALEGSV-----AIAG-AVIRWLRDNLGIIKSSE----------EIEKLAKEV--- 386
Cdd:cd24121 265 ---HEVVVDEPD-LEPEGVgytICLGVPGRWlramaNMAGtPNLDWFLRELGEVLKEGaepagsdlfqDLEELAASSppg 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 387 --GTSYGCYFVPAfsGLYAPYWEPSARGIICGLTQFTNKCHIAFAALEAVCFQTREILDAMnrdcGIPLSHLQVDGGMTS 464
Cdd:cd24121 341 aeGVLYHPYLSPA--GERAPFVNPNARAQFTGLSLEHTRADLLRAVYEGVALAMRDCYEHM----GEDPGELRLSGGGAR 414
|
490 500
....*....|....*....|....
gi 1958808298 465 NKILMQLQADILYIPVVKPSMPET 488
Cdd:cd24121 415 SDTWCQILADALGVPVRVPAGEEF 438
|
|
| ASKHA_NBD_FGGY_SHK |
cd07777 |
nucleotide-binding domain (NBD) of sedoheptulokinase (SHK) and similar proteins; SHK (EC 2.7.1. ... |
15-489 |
1.40e-27 |
|
nucleotide-binding domain (NBD) of sedoheptulokinase (SHK) and similar proteins; SHK (EC 2.7.1.14), also called heptulokinase, or carbohydrate kinase-like protein (CARKL), is encoded by the carbohydrate kinase-like (CARKL/SHPK) gene. It acts as a modulator of macrophage activation through control of glucose metabolism. SHK catalyzes the ATP-dependent phosphorylation of sedoheptulose to produce sedoheptulose 7-phosphate and ADP. The presence of Mg2+ or Mn2+ might be required for catalytic activity. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466796 [Multi-domain] Cd Length: 436 Bit Score: 115.40 E-value: 1.40e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 15 AVDQGTSSTRFLVFNSKTAELLS----HHQVEIKQEFPreGWVEQDPKEILQSVYECIEKTCEKLGqlnidiSNIKAIGV 90
Cdd:cd07777 4 GIDIGTTSIKAALLDLESGRILEsvsrPTPAPISSDDP--GRSEQDPEKILEAVRNLIDELPREYL------SDVTGIGI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 91 SNQRETTVVWDKlTGEPLYNAVAapvspgssvpvavvpsgspvpaagassvWLDLRtqSTVEKLSKRIPGNNNFvKSKTG 170
Cdd:cd07777 76 TGQMHGIVLWDE-DGNPVSPLIT----------------------------WQDQR--CSEEFLGGLSTYGEEL-LPKSG 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 171 LPLSTYFSAVKLRWLLdnvkkVQEAVEENRALFGTIDSWLIWSLTGGINggvHCTDVTNASRTMLFNIHSLEWDKELCEF 250
Cdd:cd07777 124 MRLKPGYGLATLFWLL-----RNGPLPSKADRAGTIGDYIVARLTGLPK---PVMHPTNAASWGLFDLETGTWNKDLLEA 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 251 FGIPMEILPNVRSSSEIYGlmkishSLKAGALEGVPISGCLGDQSAALVGQMCFQDGQAKNTYGTG---CFLLC-NTGHK 326
Cdd:cd07777 196 LGLPVILLPEIVPSGEIVG------TLSSALPKGIPVYVALGDNQASVLGSGLNEENDAVLNIGTGaqlSFLTPkFELSG 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 327 CV----FSEHGLLTTVAyKL--GRdkpVYYALEGSVAiagaviRWLRDnLGIIKSSEEI-EKLAKEVGTSYGC--YFVPA 397
Cdd:cd07777 270 SVeirpFFDGRYLLVAA-SLpgGR---ALAVLVDFLR------EWLRE-LGGSLSDDEIwEKLDELAESEESSdlSVDPT 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 398 FSGlyaPYWEPSARGIICGLTQ--FTNKcHIAFAALEAVCfqtREILDAMNRDC--GIPLSHLQVDGGM-TSNKILMQLQ 472
Cdd:cd07777 339 FFG---ERHDPEGRGSITNIGEsnFTLG-NLFRALCRGIA---ENLHEMLPRLDldLSGIERIVGSGGAlRKNPVLRRII 411
|
490
....*....|....*..
gi 1958808298 473 ADILYIPVVKPSMPETT 489
Cdd:cd07777 412 EKRFGLPVVLSEGSEEA 428
|
|
| ASKHA_NBD_FGGY_L-RBK |
cd07781 |
nucleotide-binding domain (NBD) of ribulokinase (RBK) and similar proteins; RBK (EC 2.7.1.16; ... |
8-489 |
1.09e-25 |
|
nucleotide-binding domain (NBD) of ribulokinase (RBK) and similar proteins; RBK (EC 2.7.1.16; also known as L-ribulokinase) catalyzes the MgATP-dependent phosphorylation of L(or D)-ribulose to produce L(or D)-ribulose 5-phosphate and ADP, which is the second step in arabinose catabolism. It also phosphorylates a variety of other sugar substrates including ribitol and arabitol. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466799 [Multi-domain] Cd Length: 504 Bit Score: 110.70 E-value: 1.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 8 VLGplvgaVDQGTSSTRFLVFNSKTAELLSHHQVEIKQEF--PREGWVEQDPKEILQSVYECIEKTCEKLGqlnIDISNI 85
Cdd:cd07781 2 VIG-----IDFGTQSVRAGLVDLADGEELASAVVPYPTGYipPRPGWAEQNPADYWEALEEAVRGALAEAG---VDPEDV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 86 KAIGVSnqreTTvvwdkltgeplynavaapvspgSSVPVAVVPSGSPV-PAAgassVWLDLRTQSTVEKLSKRIPGNNNF 164
Cdd:cd07781 74 VGIGVD----TT----------------------SSTVVPVDEDGNPLaPAI----LWMDHRAQEEAAEINETAHPALEY 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 165 VKSKTGLPLS--TYFSavKLRWLLDNVKKVQEA----VEEnralfgtIDsWLIWSLTGGINGGVhCtdvtNASRTMLFNI 238
Cdd:cd07781 124 YLAYYGGVYSseWMWP--KALWLKRNAPEVYDAaytiVEA-------CD-WINARLTGRWVRSR-C----AAGHKWMYNE 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 239 HSLEWDKELCEFFGIPM----EILP-NVRSSSEIYGLMKISHSLKAGALEGVPISGCLGDQSAALVGQMCFQDGQAKNTY 313
Cdd:cd07781 189 WGGGPPREFLAALDPGLlklrEKLPgEVVPVGEPAGTLTAEAAERLGLPAGIPVAQGGIDAHMGAIGAGVVEPGTLALIM 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 314 GT-GCFLLcnTGHKCVFSEhGLLTTVayklgrDKPV---YYALEGSVAIAGAVIRWLRDNLGI------IKSSEEIEKLA 383
Cdd:cd07781 269 GTsTCHLM--VSPKPVDIP-GICGPV------PDAVvpgLYGLEAGQSAVGDIFAWFVRLFVPpaeergDSIYALLSEEA 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 384 KEVGTsyGCyfvpafSGLYA---------PYWEPSARGIICGLTQFTNKCHIAFAALEAVCFQTREILDAMnRDCGIPLS 454
Cdd:cd07781 340 AKLPP--GE------SGLVAldwfngnrtPLVDPRLRGAIVGLTLGTTPAHIYRALLEATAFGTRAIIERF-EEAGVPVN 410
|
490 500 510
....*....|....*....|....*....|....*.
gi 1958808298 455 HLQVDGGMTS-NKILMQLQADILYIPVVKPSMPETT 489
Cdd:cd07781 411 RVVACGGIAEkNPLWMQIYADVLGRPIKVPKSDQAP 446
|
|
| ASKHA_NBD_FGGY_AI-2K |
cd07775 |
nucleotide-binding domain (NBD) of autoinducer-2 kinase (AI-2 kinase) and similar proteins; ... |
15-489 |
1.83e-24 |
|
nucleotide-binding domain (NBD) of autoinducer-2 kinase (AI-2 kinase) and similar proteins; AI-2 kinase (EC 2.7.1.189), also known as LsrK, catalyzes the phosphorylation of autoinducer-2 (AI-2) to phospho-AI-2, which subsequently inactivates the transcriptional regulator LsrR and leads to the transcription of the lsr operon. It phosphorylates the ring-open form of (S)-4,5-dihydroxypentane-2,3-dione (DPD), which is the precursor to all AI-2 signaling molecules, at the C5 position. It is required for the regulation of the lsr operon and many other genes. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466794 [Multi-domain] Cd Length: 492 Bit Score: 106.65 E-value: 1.83e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 15 AVDQGTSSTRFLVFNsKTAELLSHHQVE-IKQEFPR-EGWVEQDPKEILQSVYECIEKTCEklgQLNIDISNIKAIGVSN 92
Cdd:cd07775 4 ALDAGTGSGRAVIFD-LEGNQIAVAQREwRHKEVPDvPGSMDFDTEKNWKLICECIREALK---KAGIAPKSIAAISTTS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 93 QRETTVVWDKlTGEPLYnAVAApvspgssvpvavvpsgspvpaagassvwLDLRTQSTVEKLSKRIPGNNNFVKSKTGLP 172
Cdd:cd07775 80 MREGIVLYDN-EGEEIW-ACAN----------------------------VDARAAEEVSELKELYNTLEEEVYRISGQT 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 173 LStyFSAV-KLRWLLDNVKKVQEAVeenrALFGTIDSWLIWSLTGGInggvhCTDVTNASRTMLFNIHSLEWDKELCEFF 251
Cdd:cd07775 130 FA--LGAIpRLLWLKNNRPEIYRKA----AKITMLSDWIAYKLSGEL-----AVEPSNGSTTGLFDLKTRDWDPEILEMA 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 252 GIPMEILPNVRSSSEIYGLMKISHSLKAGALEGVPISGCLGDQSAALVGQMCFQDGQAKNTYGTGCFLLCNTGHKcVFSE 331
Cdd:cd07775 199 GLKADILPPVVESGTVIGKVTKEAAEETGLKEGTPVVVGGGDVQLGCLGLGVVRPGQTAVLGGSFWQQEVNTAAP-VTDP 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 332 HGLLTTVAYKLgrdkPVYYALEGSVAIAGAVIRWLRDNLGI----------IKSSEEIEKLAKEVGTsyGCY-FVPAFSG 400
Cdd:cd07775 278 AMNIRVNCHVI----PDMWQAEGISFFPGLVMRWFRDAFCAeekeiaerlgIDAYDLLEEMAKDVPP--GSYgIMPIFSD 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 401 L--YApYWEPSARGIIcGLTQFTNKCHIA--FAAL-EAVCFQTREILDAMNRDCGIPLSHLQVDGGMTSNKILMQLQADI 475
Cdd:cd07775 352 VmnYK-NWRHAAPSFL-NLDIDPEKCNKAtfFRAImENAAIVSAGNLERIAEFSGIFPDSLVFAGGASKGKLWCQILADV 429
|
490
....*....|....
gi 1958808298 476 LYIPVVKPSMPETT 489
Cdd:cd07775 430 LGLPVKVPVVKEAT 443
|
|
| PRK10331 |
PRK10331 |
L-fuculokinase; Provisional |
17-490 |
1.89e-21 |
|
L-fuculokinase; Provisional
Pssm-ID: 182383 [Multi-domain] Cd Length: 470 Bit Score: 97.41 E-value: 1.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 17 DQGTSSTRFLVFNSKTAELLSHHQ---VEIKQEFPRegWVEQDPKEILQSVYECIEKTCEKLGQlnidiSNIKAIGVsnq 93
Cdd:PRK10331 8 DCGATNVRAIAVDRQGKIVARASTpnaSDIAAENSD--WHQWSLDAILQRFADCCRQINSELTE-----CHIRGITV--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 94 reTTVVWDkltgeplynavaapvspgssvpvavvpsGSPVPAAGA------SsvWLDLRTQSTVEKLSKRIPGNNNFVKS 167
Cdd:PRK10331 78 --TTFGVD----------------------------GALVDKQGNllypiiS--WKCPRTAAVMENIERYISAQQLQQIS 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 168 KTG-LPLSTYFsavKLRWLldnvkkvqeavEENRA-LFGTIDSWL-IWSLtggIN---GGVHCTDVTNASRTMLFNIHSL 241
Cdd:PRK10331 126 GVGaFSFNTLY---KLVWL-----------KENHPqLLEQAHAWLfISSL---INhrlTGEFTTDITMAGTSQMLDIQQR 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 242 EWDKELCEFFGIPMEILPNVRSSSEIYGLMKISHSLKAGALEGVPISGCLGDQSAALVGQMCFQDgQAKNTYGTGCFLLC 321
Cdd:PRK10331 189 DFSPEILQATGLSRRLFPRLVEAGEQIGTLQPSAAALLGLPVGIPVISAGHDTQFALFGSGAGQN-QPVLSSGTWEILMV 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 322 NTGH---KCVFSEHGLLTTVAYKLGRDKPvyyaleGSVAIAGAVIRWLRDNLGiikSSEE-----IEKlAKEVGT-SYGC 392
Cdd:PRK10331 268 RSAQvdtSLLSQYAGSTCELDSQSGLYNP------GMQWLASGVLEWVRKLFW---TAETpyqtmIEE-ARAIPPgADGV 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 393 YFVPAFSGlyapywepSARGIICGLTQFTNKCHIAFAALEAVCFQTREILDAMNRDCGIPLSHLQVDGGMTSNKILMQLQ 472
Cdd:PRK10331 338 KMQCDLLA--------CQNAGWQGVTLNTTRGHFYRAALEGLTAQLKRNLQVLEKIGHFKASELLLVGGGSRNALWNQIK 409
|
490
....*....|....*...
gi 1958808298 473 ADILYIPVVKPSMPETTA 490
Cdd:PRK10331 410 ANMLDIPIKVLDDAETTV 427
|
|
| ASKHA_NBD_FGGY_RBK-like |
cd07768 |
nucleotide-binding domain (NBD) of ribulokinase-like carbohydrate kinases; The RBK family ... |
16-488 |
1.11e-18 |
|
nucleotide-binding domain (NBD) of ribulokinase-like carbohydrate kinases; The RBK family includes bacterial RBK, vertebrate D-ribulokinase FGGY (also known as FGGY carbohydrate kinase domain-containing protein), Saccharomyces cerevisiae D-ribulokinase YDR109C, and Yersinia Pseudotuberculosis uncharacterized carbohydrate kinase that has been named glyerol/xylulose kinase. RBK (EC 2.7.1.16; also known as L-ribulokinase) catalyzes the MgATP-dependent phosphorylation of L(or D)-ribulose to produce L(or D)-ribulose 5-phosphate and ADP, which is the second step in arabinose catabolism. It also phosphorylates a variety of other sugar substrates including ribitol and arabitol. D-ribulokinase (EC 2.7.1.47) catalyzes ATP-dependent phosphorylation of D-ribulose at C-5 to form D-ribulose 5-phosphate. It is postulated to function in a metabolite repair mechanism by preventing toxic accumulation of free D-ribulose formed by non-specific phosphatase activities. Alternatively, D-ribulokinase may play a role in regulating D-ribulose 5-phosphate recycling in the pentose phosphate pathway. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466788 [Multi-domain] Cd Length: 522 Bit Score: 89.22 E-value: 1.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 16 VDQGTSSTRFLVFNSKTAELLSHHQVEIKQ-EFPREGWVEQDPKEILQSVYECIEKTcekLGQLNIDISNIKAIGVSNQR 94
Cdd:cd07768 5 VDVGTSSARAGVYDLYAGLEMAQEPVPYYQdSSKKSWKFWQKSTEIIKALQKCVQKL---NIREGVDAYEVKGCGVDATC 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 95 eTTVVWDKlTGEPlyNAVAAPVSPGSSVpvavvpsgspvpaagasSVWLDLRTQSTVEKLskripgnnNFVKSKTGLP-- 172
Cdd:cd07768 82 -SLAIFDR-EGTP--LMALIPYPNEDNV-----------------IFWMDHSAVNEAQWI--------NMQCPQQLLDyl 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 173 ---LSTYFSAVKLRWLLDNVKKVQEAVEEnraLFGTIDsWLIWSLTGGINGGVhCTDVTNASrtmlFNIHSLEWDKELCE 249
Cdd:cd07768 133 ggkISPEMGVPKLKYFLDEYSHLRDKHFH---IFDLHD-YIAYELTRLYEWNI-CGLLGKEN----LDGEESGWSSSFFK 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 250 FFGIPME------ILPNVRSSSEIYGLMKISHSLKAGALEGVPISGCLGDQSAALVgqmcfqdGQAKNTYGTGCFLLCNT 323
Cdd:cd07768 204 NIDPRLEhltttkNLPSNVPIGTTSGVALPEMAEKMGLHPGTAVVVSCIDAHASWF-------AVASPHLETSLFMIAGT 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 324 GhkcvfSEHGLLTTVAYKL-GRDKPVYYAL-------EGSVAIAGAVIRWL-------RDNLGIIKSSEEI--------E 380
Cdd:cd07768 277 S-----SCHMYGTTISDRIpGVWGPFDTIIdpdysvyEAGQSATGKLIEHLfeshpcaRKFDEALKKGADIyqvleqtiR 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 381 KLAKEVGTSYGCYFVPAFSGLYAPYWEPSARGIICGLTQFT---NKCHIAFAALEAVCFQTREILDAMNRDcGIPLSHLQ 457
Cdd:cd07768 352 QIEKNNGLSIHILTLDMFFGNRSEFADPRLKGSFIGESLDTsmlNLTYKYIAILEALAFGTRLIIDTFQNE-GIHIKELR 430
|
490 500 510
....*....|....*....|....*....|.
gi 1958808298 458 VDGGMTSNKILMQLQADILYIPVVKPSMPET 488
Cdd:cd07768 431 ASGGQAKNERLLQLIALVTNVAIIKPKENMM 461
|
|
| PRK15027 |
PRK15027 |
xylulokinase; Provisional |
16-475 |
1.33e-17 |
|
xylulokinase; Provisional
Pssm-ID: 184987 [Multi-domain] Cd Length: 484 Bit Score: 85.79 E-value: 1.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 16 VDQGTSSTRFLVFNSKtAELLSHHQVEIKQEFPREGWVEQDPKEILQSVyeciEKTCEKLGQLNiDISNIKAIGVSNQRE 95
Cdd:PRK15027 5 IDLGTSGVKVILLNEQ-GEVVASQTEKLTVSRPHPLWSEQDPEQWWQAT----DRAMKALGDQH-SLQDVKALGIAGQMH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 96 TTVVWDKltgeplYNAVAAPvspgssvpvavvpsgspvpaagaSSVWLDLRTQSTVEKLSKRIPGNnnfvKSKTGLPLST 175
Cdd:PRK15027 79 GATLLDA------QQRVLRP-----------------------AILWNDGRCAQECALLEARVPQS----RVITGNLMMP 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 176 YFSAVKLRWlldnVKKVQEAVEENRALFGTIDSWLIWSLTGginggVHCTDVTNASRTMLFNIHSLEWDKELCEFFGIPM 255
Cdd:PRK15027 126 GFTAPKLLW----VQRHEPEIFRQIDKVLLPKDYLRLRMTG-----EFASDMSDAAGTMWLDVAKRDWSDVMLQACHLSR 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 256 EILPNVRSSSEIYGLMkISHSLKAGALEGVPISGCLGDQSAALVGQMCFQDGQAKNTYGTgcfllcnTGHKCVFSEhGLL 335
Cdd:PRK15027 197 DQMPALYEGSEITGAL-LPEVAKAWGMATVPVVAGGGDNAAGAVGVGMVDANQAMLSLGT-------SGVYFAVSE-GFL 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 336 T---TVAYKLGRDKPVYYALEGSVAIAGAVIRW------LRDNLGIIKSSEEIEKLAKEVgtsygcYFVPAFSGLYAPYW 406
Cdd:PRK15027 268 SkpeSAVHSFCHALPQRWHLMSVMLSAASCLDWaakltgLSNVPALIAAAQQADESAEPV------WFLPYLSGERTPHN 341
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958808298 407 EPSARGIICGLTQFTNKCHIAFAALEAVCFQTREILDAMNrDCGIPLSHLQVDGGMTSNKILMQLQADI 475
Cdd:PRK15027 342 NPQAKGVFFGLTHQHGPNELARAVLEGVGYALADGMDVVH-ACGIKPQSVTLIGGGARSEYWRQMLADI 409
|
|
| ASKHA_NBD_FGGY_D-RBK |
cd07782 |
nucleotide-binding domain (NBD) of D-ribulokinase FGGY and similar proteins; The subfamily ... |
15-488 |
1.77e-16 |
|
nucleotide-binding domain (NBD) of D-ribulokinase FGGY and similar proteins; The subfamily includes vertebrate D-ribulokinase FGGY (also known as FGGY carbohydrate kinase domain-containing protein) and similar proteins, such as Saccharomyces cerevisiae D-ribulokinase YDR109C, Yersinia Pseudotuberculosis uncharacterized carbohydrate kinase that has been named glyerol/xylulose kinase. D-ribulokinase (EC 2.7.1.47) catalyzes ATP-dependent phosphorylation of D-ribulose at C-5 to form D-ribulose 5-phosphate. It is postulated to function in a metabolite repair mechanism by preventing toxic accumulation of free D-ribulose formed by non-specific phosphatase activities. Alternatively, D-ribulokinase may play a role in regulating D-ribulose 5-phosphate recycling in the pentose phosphate pathway.
Pssm-ID: 466800 [Multi-domain] Cd Length: 540 Bit Score: 82.58 E-value: 1.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 15 AVDQGTSSTRFLVFNSkTAELLSHHQVEIKQEFPREGWVEQDPKEILQSVYECIEKTCEKLGqlnIDISNIKAIGVsnqr 94
Cdd:cd07782 4 GVDVGTGSARAGLFDL-DGRLLATASQPITTWNPKPDFYEQSSEDIWQAVCEAVKEVLEGAG---VDPEQVKGIGF---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 95 ETT---VVWDKlTGEPlynavaapvspgssvpVAVVPSGSP----VpaagassVWLDLRTQSTVEklskRIpgnnnfvkS 167
Cdd:cd07782 76 DATcslVVLDA-EGKP----------------VSVSPSGDDernvI-------LWMDHRAVEEAE----RI--------N 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 168 KTGLPLSTYFSAV--------KLRWLldnvKKVQEAVEENRALFGTIDSWLIWSLTGGINGGVhCTDVtnASRTMLFNIH 239
Cdd:cd07782 120 ATGHEVLKYVGGKispemeppKLLWL----KENLPETWAKAGHFFDLPDFLTWKATGSLTRSL-CSLV--CKWTYLAHEG 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 240 SLE-WDKELCEFFG-----------IPMEILPNVRSSSEiyGLmkishSLKA----GALEGVPIS--------GCLGDQS 295
Cdd:cd07782 193 SEGgWDDDFFKEIGledlvednfakIGSVVLPPGEPVGG--GL-----TAEAakelGLPEGTPVGvslidahaGGLGTLG 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 296 AALVGQMC-FQDGQAKntygtgCFLLCNTG--HkCVFSEHGLLttVA-----YKlGRDKPVYYALEGSVAIAGAVIRWlr 367
Cdd:cd07782 266 ADVGGLPCeADPLTRR------LALICGTSscH-MAVSPEPVF--VPgvwgpYY-SAMLPGLWLNEGGQSATGALLDH-- 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 368 dnlgIIKS---SEEIEKLAKEVGTSY------------------------GCYFVPAFSGLYAPYWEPSARGIICGLTQF 420
Cdd:cd07782 334 ----IIEThpaYPELKEEAKAAGKSIyeylnerleqlaeekglplayltrDLHVLPDFHGNRSPLADPTLRGMISGLTLD 409
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958808298 421 TNKCHIA---FAALEAVCFQTREILDAMNRdCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPET 488
Cdd:cd07782 410 TSLDDLAllyLATLQALAYGTRHIIEAMNA-AGHKIDTIFMCGGLSKNPLFVQLHADVTGCPVVLPKEPEA 479
|
|
| ASKHA_NBD_FGGY_RhaB-like |
cd07771 |
nucleotide-binding domain (NBD) of rhamnulokinase (RhaB) and similar proteins; Rhamnulokinase ... |
144-481 |
3.15e-16 |
|
nucleotide-binding domain (NBD) of rhamnulokinase (RhaB) and similar proteins; Rhamnulokinase (EC 2.7.1.5), also known as L-rhamnulose kinase, ATP:L-rhamnulose phosphotransferase, L-rhamnulose 1-kinase, or rhamnulose kinase, is an enzyme involved in the second step in rhamnose catabolism. It catalyzes the ATP-dependent phosphorylation of L-rhamnulose to produce L-rhamnulose-1-phosphate and ADP. Rhamnulokinase exists as a monomer composed of two large domains. The ATP binding site is located in the cleft between the two domains. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain. The presence of divalent Mg2+ or Mn2+ is required for catalysis. The subfamily also includes Streptococcus pneumoniae L-fuculose k fuculose Kinase inase (FcsK) that uses ATP to phosphorylate fuculose creating fuculose-1-phosphate, and Alkalihalobacillus clausii bifunctional enzyme RhaA/RhaB. Members of this subfamily belong to the FGGY family of carbohydrate kinases.
Pssm-ID: 466791 [Multi-domain] Cd Length: 460 Bit Score: 81.42 E-value: 3.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 144 DLRTQSTVEKLSKRIPGNNNFvkSKTGLPLSTYFSAVKLRWLldnvkkvqeaVEENRALFGTIDSWLI------WSLTGG 217
Cdd:cd07771 98 DPRTEGMMEELFEKISKEELY--ERTGIQFQPINTLYQLYAL----------KKEGPELLERADKLLMlpdllnYLLTGE 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 218 InggvhCTDVTNASRTMLFNIHSLEWDKELCEFFGIPMEILPNVRSSSEIYGLMKISHSlKAGALEGVP-ISGCLGDQSA 296
Cdd:cd07771 166 K-----VAEYTIASTTQLLDPRTKDWSEELLEKLGLPRDLFPPIVPPGTVLGTLKPEVA-EELGLKGIPvIAVASHDTAS 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 297 ALVGQMCFQDGQAkntygtgcFLLCNT----GhkcVFSEHGLLTTVAYKLGrdkpvyYALEGSVA--------IAGaviR 364
Cdd:cd07771 240 AVAAVPAEDEDAA--------FISSGTwsliG---VELDEPVITEEAFEAG------FTNEGGADgtirllknITG---L 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 365 WL----RDNL---GIIKSSEEIEKLAKEVgTSYGCYFVPAFSGLYAPywePSARGIICGLTQFTN------KCHIAFAAL 431
Cdd:cd07771 300 WLlqecRREWeeeGKDYSYDELVALAEEA-PPFGAFIDPDDPRFLNP---GDMPEAIRAYCRETGqpvpesPGEIARCIY 375
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1958808298 432 EAVCFQTREILDAMNRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVV 481
Cdd:cd07771 376 ESLALKYAKTIEELEELTGKRIDRIHIVGGGSRNALLCQLTADATGLPVI 425
|
|
| AraB |
COG1069 |
Ribulose kinase [Carbohydrate transport and metabolism]; |
5-492 |
1.01e-13 |
|
Ribulose kinase [Carbohydrate transport and metabolism];
Pssm-ID: 440687 [Multi-domain] Cd Length: 532 Bit Score: 73.61 E-value: 1.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 5 KKAVLGplvgaVDQGTSSTRFLVFNSKTAELLSHHQVEIKQ------EFPREGWVEQDPKEILQSVYECIektCEKLGQL 78
Cdd:COG1069 1 EKYVIG-----VDFGTDSVRAVVVDAADGEELASAVHPYPRwviglyLPPPPDQARQHPLDYLEALEAAV---REALAQA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 79 NIDISNIKAIGVSNQRETTVVWDKlTGEPLynavaaPVSPG-SSVPVA-VVpsgspvpaagassVWLDLRTQSTVEklsk 156
Cdd:COG1069 73 GVDPADVVGIGVDATGCTPVPVDA-DGTPL------ALLPEfAENPHAmVI-------------LWKDHTAQEEAE---- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 157 RIpgnnNFVKSKTGLPLSTY---------FSAvKLRWLLdnvkkvqeavEENRALFGTIDS------WLIWSLTGGINGG 221
Cdd:COG1069 129 RI----NELAKARGEDYLRYvggiissewFWP-KILHLL----------REDPEVYEAADSfvelcdWITWQLTGSLKRS 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 222 VhCTdvtnASRTMLFNIHSLEWDKElcEFF---GIPMEILPNvRSSSEIYGLmkishSLKAGAL-----------EGVPI 287
Cdd:COG1069 194 R-CT----AGHKALWHAHEGGYPSE--EFFaalDPLLDGLAD-RLGTEIYPL-----GEPAGTLtaewaarlglpPGTAV 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 288 SGCLGDQSAALVGQMCFQDGQ-AKNtYGT-GCFLLCNTGHKC-------VFSehGLLttvayklgrdkPVYYALEGSVAI 358
Cdd:COG1069 261 AVGAIDAHAGAVGAGGVEPGTlVKV-MGTsTCHMLVSPEERFvpgicgqVDG--SIV-----------PGMWGYEAGQSA 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 359 AGAVIRWLRDNLGiikSSEEIEKLAKEVGTS----------------YGCYFVPAFSGLYAPYWEPSARGIICGLTQFTN 422
Cdd:COG1069 327 VGDIFAWFVRLLV---PPLEYEKEAEERGISlhpllteeaaklppgeSGLHALDWFNGNRSPLADQRLKGVILGLTLGTD 403
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958808298 423 KCHIAFAALEAVCFQTREILDAMNrDCGIPLSHLQVDGG-MTSNKILMQLQADILYIPVVKPSMPETTALG 492
Cdd:COG1069 404 AEDIYRALVEATAFGTRAIIERFE-EEGVPIDEIIACGGiATKNPLVMQIYADVTGRPIKVAASEQACALG 473
|
|
| PRK10939 |
PRK10939 |
autoinducer-2 (AI-2) kinase; Provisional |
15-292 |
1.22e-08 |
|
autoinducer-2 (AI-2) kinase; Provisional
Pssm-ID: 182853 [Multi-domain] Cd Length: 520 Bit Score: 57.71 E-value: 1.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 15 AVDQGTSSTRFLVFNSKTAELLSHHQVEIKQEFPR-EGWVEQDPKEILQSVYECIEktcEKLGQLNIDISNIKAIGVSNQ 93
Cdd:PRK10939 7 ALDAGTGSIRAVIFDLNGNQIAVGQAEWRHLAVPDvPGSMEFDLEKNWQLACQCIR---QALQKAGIPASDIAAVSATSM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 94 RETTVVWDKlTGEPLYnAVAApvspgssvpvavvpsgspvpaagassvwLDLRTQSTVEKLSKRIPGNNNFVKSKTGLPL 173
Cdd:PRK10939 84 REGIVLYDR-NGTEIW-ACAN----------------------------VDARASREVSELKELHNNFEEEVYRCSGQTL 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 174 StyFSAV-KLRWLldnvKKVQEAVEENRALFGTIDSWLIWSLTGGInggvhCTDVTNASRTMLFNIHSLEWDKELCEFFG 252
Cdd:PRK10939 134 A--LGALpRLLWL----AHHRPDIYRQAHTITMISDWIAYMLSGEL-----AVDPSNAGTTGLLDLVTRDWDPALLEMAG 202
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1958808298 253 IPMEILPNVRSSSEIYGLMKISHSLKAGALEGVPI--------SGCLG 292
Cdd:PRK10939 203 LRADILPPVKETGTVLGHVTAKAAAETGLRAGTPVvmgggdvqLGCLG 250
|
|
| ASKHA_NBD_FGGY_MPA43-like |
cd07778 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae protein MPA43 and similar proteins; ... |
16-482 |
2.96e-07 |
|
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae protein MPA43 and similar proteins; This subfamily contains a group of uncharacterized proteins with similarity to Saccharomyces cerevisiae protein MPA43. They belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466797 [Multi-domain] Cd Length: 544 Bit Score: 53.18 E-value: 2.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 16 VDQGTSSTRFLVFNSKTaELLSHHQVEI-KQEFPREGW-VEQDPKEILQSVYECIEKTCEKLGQLNIDISNIKA---IGV 90
Cdd:cd07778 5 IDVGSTSVRIGIFDYHG-TLLATSERPIsYKQDPKDLWfVTQSSTEIWKAIKTALKELIEELSDYIVSGIGVSAtcsMVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 91 SNQRETTvvwDKLTgePlYNAVAAPVSPGSSVpvavvpsgspvpaagasSVWLDLRTQSTVEKLskripgNNNFVKSKTG 170
Cdd:cd07778 84 MQRDSDT---SYLV--P-YNVIHEKSNPDQDI-----------------IFWMDHRASEETQWL------NNILPDDILD 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 171 LPLSTYF---SAVKLRWLLDNVKkvqEAVEENRALFGTIDsWLIWSL-TGGINGGVhcTDVTNASRTMLFNIHSLE-WDK 245
Cdd:cd07778 135 YLGGGFIpemAIPKLKYLIDLIK---EDTFKKLEVFDLHD-WISYMLaTNLGHSNI--VPVNAPPSIGIGIDGSLKgWSK 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 246 ELCEFFGIPMEILPNVRSSSEIYGLM----KISH-SLKAGALEGVPIS-----GCLgDQSAALVGQMC---FQDGQAKNT 312
Cdd:cd07778 209 DFYSKLKISTKVCNVGNTFKEAPPLPyagiPIGKvNVILASYLGIDKStvvghGCI-DCYAGWFSTFAaakTLDTTLFMV 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 313 YGTG-CFLLcntGHKCV-----------FSEhgllttvaykLGRDKPVYyalEGSVAIAG-----------AVIRWLRDN 369
Cdd:cd07778 288 AGTStCFLY---ATSSSqvgpipgiwgpFDQ----------LLKNYSVY---EGGQSATGklieklfnshpAIIELLKSD 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 370 LGIIKSSEE-IEKLAKEVGTS----YGCYFvpaFSGLYA----PYWEPSARGIICGLTQFTNKCHIAF---AALEAVCFQ 437
Cdd:cd07778 352 ANFFETVEEkIDKYERLLGQSihylTRHMF---FYGDYLgnrtPYNDPNMSGSFIGESTDSSLTDLVLkyiLILEFLAFQ 428
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1958808298 438 TREILDAMNRDCgIPLSHLQVDGGMTSNKILMQLQADILYIPVVK 482
Cdd:cd07778 429 TKLIIDNFQKEK-IIIQKVVISGSQAKNARLLQLLSTVLSKIHII 472
|
|
| PRK04123 |
PRK04123 |
ribulokinase; Provisional |
411-492 |
2.21e-04 |
|
ribulokinase; Provisional
Pssm-ID: 235221 [Multi-domain] Cd Length: 548 Bit Score: 44.07 E-value: 2.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958808298 411 RGIICGLTQFTNKCHIAFAALEAVCFQTREILDAMnRDCGIPLSHLQVDGGM-TSNKILMQLQADILYIPV-VKPSmPET 488
Cdd:PRK04123 398 KGVITGLTLGTDAPDIYRALIEATAFGTRAIMECF-EDQGVPVEEVIAAGGIaRKNPVLMQIYADVLNRPIqVVAS-DQC 475
|
....
gi 1958808298 489 TALG 492
Cdd:PRK04123 476 PALG 479
|
|
| rhaB |
PRK10640 |
rhamnulokinase; Provisional |
206-254 |
2.77e-03 |
|
rhamnulokinase; Provisional
Pssm-ID: 182609 [Multi-domain] Cd Length: 471 Bit Score: 40.47 E-value: 2.77e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1958808298 206 IDSWLIWSLTGGINggvhcTDVTNASRTMLFNIHSLEWDKELCEFFGIP 254
Cdd:PRK10640 142 IPDYFSYRLTGKMN-----WEYTNATTTQLVNINSDDWDESLLAWSGAP 185
|
|
| |
